+Open data
-Basic information
Entry | Database: PDB / ID: 1jei | ||||||
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Title | LEM DOMAIN OF HUMAN INNER NUCLEAR MEMBRANE PROTEIN EMERIN | ||||||
Components | EMERIN | ||||||
Keywords | MEMBRANE PROTEIN / emerin nucleus membrane domain dystrophy | ||||||
Function / homology | Function and homology information TMEM240-body / nuclear membrane organization / Depolymerization of the Nuclear Lamina / Nuclear Envelope Breakdown / Initiation of Nuclear Envelope (NE) Reformation / RHOD GTPase cycle / nuclear outer membrane / regulation of canonical Wnt signaling pathway / muscle organ development / nuclear inner membrane ...TMEM240-body / nuclear membrane organization / Depolymerization of the Nuclear Lamina / Nuclear Envelope Breakdown / Initiation of Nuclear Envelope (NE) Reformation / RHOD GTPase cycle / nuclear outer membrane / regulation of canonical Wnt signaling pathway / muscle organ development / nuclear inner membrane / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / beta-tubulin binding / skeletal muscle cell differentiation / RHOG GTPase cycle / RAC3 GTPase cycle / RAC2 GTPase cycle / negative regulation of fibroblast proliferation / RAC1 GTPase cycle / positive regulation of protein export from nucleus / muscle contraction / negative regulation of canonical Wnt signaling pathway / spindle / cellular response to growth factor stimulus / nuclear envelope / actin binding / nuclear membrane / microtubule / cadherin binding / endoplasmic reticulum / nucleoplasm / membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Method | SOLUTION NMR / semi-automated iterative procedure using X-PLOR, home-written C-shell programs | ||||||
Authors | Wolff, N. / Gilquin, B. / Courchay, K. / Callebaut, I. / Zinn-Justin, S. | ||||||
Citation | Journal: FEBS LETT. / Year: 2001 Title: Structural analysis of emerin, an inner nuclear membrane protein mutated in X-linked Emery-Dreifuss muscular dystrophy Authors: Wolff, N. / Gilquin, B. / Courchay, K. / Callebaut, I. / Worman, H.J. / Zinn-Justin, S. #1: Journal: Structure / Year: 2001 Title: Structural characterization of the LEM motif common to three human inner nuclar membrane proteins. Authors: Laguri, C. / Gilquin, B. / Wolff, N. / Romi-Lebrun, R. / Courchay, K. / Callebaut, I. / Worman, H.J. / Zinn-Justin, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jei.cif.gz | 173.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jei.ent.gz | 149 KB | Display | PDB format |
PDBx/mmJSON format | 1jei.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/je/1jei ftp://data.pdbj.org/pub/pdb/validation_reports/je/1jei | HTTPS FTP |
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-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 | Mass: 6237.948 Da / Num. of mol.: 1 / Fragment: LEM DOMAIN (RESIDUES 2-54) / Source method: obtained synthetically / Details: chemical synthesis / References: UniProt: P50402 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: 2D NOESY |
-Sample preparation
Details | Contents: LEM domain of emerin 1mM Solvent system: NaH2PO4/Na2HPO4 20mM, pH 6.3, 90% H2O/10% D2O or 100% D2O |
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Sample conditions | Ionic strength: 20mM / pH: 6.3 / 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 |
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-Processing
NMR software |
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Refinement | Method: semi-automated iterative procedure using X-PLOR, home-written C-shell programs 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: 10 |