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Open data
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Basic information
Entry | Database: PDB / ID: 1jei | ||||||
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Title | LEM DOMAIN OF HUMAN INNER NUCLEAR MEMBRANE PROTEIN EMERIN | ||||||
![]() | EMERIN![]() | ||||||
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Function / homology | ![]() 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 / nuclear inner membrane / muscle organ development ...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 / nuclear inner membrane / muscle organ development / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Method | ![]() | ||||||
![]() | Wolff, N. / Gilquin, B. / Courchay, K. / Callebaut, I. / Zinn-Justin, S. | ||||||
![]() | ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 176.7 KB | Display | ![]() |
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PDB format | ![]() | 144.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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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: ![]() |
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NMR experiment | Type![]() ![]() |
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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 |