+Open data
-Basic information
Entry | Database: PDB / ID: 2rmy | ||||||
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Title | Structure of the N-terminal BARpeptide in SDS micelles | ||||||
Components | Myc box-dependent-interacting protein 1 | ||||||
Keywords | ENDOCYTOSIS / BARpeptide / micelle / NMR-structure / Alternative splicing / Anti-oncogene / Cell cycle / Coiled coil / Cytoplasm / Developmental protein / Differentiation / Host-virus interaction / Nucleus / Phosphoprotein / SH3 domain | ||||||
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 / molecular dynamics | ||||||
Authors | Loew, C. / Weininger, U. / Balbach, J. | ||||||
Citation | Journal: Biophys.J. / Year: 2008 Title: Structure and dynamics of helix-0 of the N-BAR domain in lipid micelles and bilayers Authors: Low, C. / Weininger, U. / Lee, H. / Schweimer, K. / Neundorf, I. / Beck-Sickinger, A.G. / Pastor, R.W. / Balbach, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2rmy.cif.gz | 109.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2rmy.ent.gz | 93.5 KB | Display | PDB format |
PDBx/mmJSON format | 2rmy.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rm/2rmy ftp://data.pdbj.org/pub/pdb/validation_reports/rm/2rmy | 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/peptide | Mass: 3714.424 Da / Num. of mol.: 1 / Fragment: UNP residues 1-33 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / Strain (production host): K12 / Variant (production host): BL21 / References: UniProt: O00499 |
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Sequence details | C-TERMINAL TYROSIN 34 FOR CONCENTRAT |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1mM [U-100% 15N] protein, 90% H2O/10% D2O / Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 1 mM / Component: entity / Isotopic labeling: [U-100% 15N] |
Sample conditions | Ionic strength: 0 / pH: 7.4 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz |
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-Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 | ||||||||||||
NMR constraints | NOE constraints total: 683 | ||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 30 / Conformers submitted total number: 10 |