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Yorodumi- PDB-1muz: NMR STRUCTURE OF THE TUMOR SUPPRESSOR BIN1: ALTERNATIVE SPLICING ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1muz | ||||||
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Title | NMR STRUCTURE OF THE TUMOR SUPPRESSOR BIN1: ALTERNATIVE SPLICING IN MELANOMA AND INTERACTION WITH C-MYC | ||||||
Components | Myc box dependent interacting protein 1 | ||||||
Keywords | ENDOCYTOSIS/EXOCYTOSIS / TUMOR SUPPRESSOR / ENDOCYTOSIS-EXOCYTOSIS COMPLEX | ||||||
Function / homology | Function and homology information lipid tube / negative regulation of ventricular cardiac muscle cell action potential / negative regulation of calcium ion transmembrane transport via high voltage-gated calcium channel / negative regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process / lipid tube assembly / RNA polymerase II transcription repressor complex / regulation of cell cycle process / T-tubule organization / negative regulation of potassium ion transmembrane transport / varicosity ...lipid tube / negative regulation of ventricular cardiac muscle cell action potential / negative regulation of calcium ion transmembrane transport via high voltage-gated calcium channel / negative regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process / lipid tube assembly / RNA polymerase II transcription repressor complex / regulation of cell cycle process / T-tubule organization / negative regulation of potassium ion transmembrane transport / varicosity / extrinsic component of synaptic vesicle membrane / axon initial segment / cerebellar mossy fiber / positive regulation of astrocyte differentiation / nucleus localization / node of Ranvier / aspartic-type endopeptidase inhibitor activity / I band / RNA polymerase binding / nucleus organization / regulation of neuron differentiation / clathrin binding / positive regulation of actin filament polymerization / endosome to lysosome transport / regulation of heart rate by cardiac conduction / positive regulation of endocytosis / negative regulation of amyloid-beta formation / synaptic vesicle endocytosis / axon terminus / cytoskeleton organization / T-tubule / phospholipid binding / tau protein binding / Z disc / endocytosis / actin filament binding / synaptic vesicle / actin cytoskeleton / GTPase binding / Clathrin-mediated endocytosis / nuclear envelope / protein-folding chaperone binding / protease binding / vesicle / endosome / positive regulation of apoptotic process / axon / dendrite / glutamatergic synapse / negative regulation of transcription by RNA polymerase II / membrane / identical protein binding / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Pineda-Lucena, A. / Arrowsmith, C.H. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2005 Title: A structure-based model of the c-Myc/Bin1 protein interaction shows alternative splicing of Bin1 and c-Myc phosphorylation are key binding determinants. Authors: Pineda-Lucena, A. / Ho, C.S. / Mao, D.Y. / Sheng, Y. / Laister, R.C. / Muhandiram, R. / Lu, Y. / Seet, B.T. / Katz, S. / Szyperski, T. / Penn, L.Z. / Arrowsmith, C.H. | ||||||
History |
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Remark 999 | SEQUENCE The protein crystallized by the author contains Lys465 which corresponds to Glu576 in the ...SEQUENCE The protein crystallized by the author contains Lys465 which corresponds to Glu576 in the Swiss-Prot entry O00499. This residue conflict is noted in the database reference. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1muz.cif.gz | 499.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1muz.ent.gz | 434.7 KB | Display | PDB format |
PDBx/mmJSON format | 1muz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mu/1muz ftp://data.pdbj.org/pub/pdb/validation_reports/mu/1muz | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 9356.479 Da / Num. of mol.: 1 / Fragment: residues 513-593 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pET15b / Production host: Escherichia coli (E. coli) / References: UniProt: O00499 |
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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 3D HETERONUCLEAR NMR TECHNIQUES |
-Sample preparation
Details | Contents: 1.5 mM Bin1(402-482) U-15N, 13C 25 mM sodium phosphate buffer, 150 mM NaCl, 1 mM DTT, 95% H2O, 5% D2O pH=6.5 Solvent system: 95% H2O/5% D2O |
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Sample conditions | Ionic strength: 300e-3 / pH: 6.5 / Pressure: ambient / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian UNITY / Manufacturer: Varian / Model: UNITY / Field strength: 600 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 lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |