+Open data
-Basic information
Entry | Database: PDB / ID: 2dig | ||||||
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Title | Solusion structure of the Todor domain of human Lamin-B receptor | ||||||
Components | Lamin-B receptor | ||||||
Keywords | DNA BINDING PROTEIN / Tudor domain / Integral nuclear envelope inner membrane protein / Nuclear protein / Receptor / structural genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information Delta14-sterol reductase / delta14-sterol reductase activity / : / neutrophil differentiation / sterol biosynthetic process / oxidoreductase activity, acting on the CH-CH group of donors / chromo shadow domain binding / Cholesterol biosynthesis / lamin binding / Initiation of Nuclear Envelope (NE) Reformation ...Delta14-sterol reductase / delta14-sterol reductase activity / : / neutrophil differentiation / sterol biosynthetic process / oxidoreductase activity, acting on the CH-CH group of donors / chromo shadow domain binding / Cholesterol biosynthesis / lamin binding / Initiation of Nuclear Envelope (NE) Reformation / nuclear inner membrane / cholesterol biosynthetic process / Regulation of MECP2 expression and activity / NADPH binding / nuclear envelope / nuclear membrane / membrane => GO:0016020 / endoplasmic reticulum membrane / DNA binding / RNA binding / membrane / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Yoneyama, M. / Tochio, N. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solusion structure of the Todor domain of human Lamin-B receptor Authors: Yoneyama, M. / Tochio, N. / 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 | 2dig.cif.gz | 392.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2dig.ent.gz | 329.1 KB | Display | PDB format |
PDBx/mmJSON format | 2dig.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/di/2dig ftp://data.pdbj.org/pub/pdb/validation_reports/di/2dig | HTTPS FTP |
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-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: 7368.020 Da / Num. of mol.: 1 / Fragment: Tudor domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: Cell-free protein synthesis / Gene: LBR / Plasmid: P050905-15 / Production host: Cell free synthesis / References: UniProt: Q14739 |
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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: 1.17mM Tudor domain U-15N,13C; 20mM d-Tris HCl (pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120 / pH: 7.0 / Pressure: ambient / Temperature: 296 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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-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: target function,structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 |