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Yorodumi- PDB-1jjx: Solution Structure of Recombinant Human Brain-type Fatty acid Bin... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1jjx | ||||||
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Title | Solution Structure of Recombinant Human Brain-type Fatty acid Binding Protein | ||||||
Components | BRAIN-TYPE FATTY ACID BINDING PROTEIN | ||||||
Keywords | LIPID BINDING PROTEIN / BETA BARREL / FATTY ACID CARRIER / 15N ISOTOPE ENRICHMENT / NMR SPECTROSCOPY | ||||||
Function / homology | Function and homology information NOTCH3 Intracellular Domain Regulates Transcription / Triglyceride catabolism / fatty acid transport / epithelial cell proliferation / fatty acid binding / nervous system development / negative regulation of cell population proliferation / lipid binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / TORSION ANGLE DYNAMICS, SIMULATED ANNEALING, ENERGY MINIMIZATION | ||||||
Authors | Rademacher, M. / Zimmerman, A.W. / Rueterjans, H. / Veerkamp, J.H. / Luecke, C. | ||||||
Citation | Journal: Mol.Cell.Biochem. / Year: 2002 Title: Solution structure of fatty acid-binding protein from human brain. Authors: Rademacher, M. / Zimmerman, A.W. / Ruterjans, H. / Veerkamp, J.H. / Lucke, C. #1: Journal: J.Biol.Chem. / Year: 2000 Title: Crystal Structure and Thermodynamic Analysis of Human Brain Fatty Acid-Binding Protein Authors: Balendiran, G.K. / Schnuetgen, F. / Scapin, G. / Boerchers, T. / Xhong, N. / Lim, K. / Godbout, R. / Spener, F. / Sacchettini, J.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jjx.cif.gz | 812.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jjx.ent.gz | 702.9 KB | Display | PDB format |
PDBx/mmJSON format | 1jjx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jj/1jjx ftp://data.pdbj.org/pub/pdb/validation_reports/jj/1jjx | 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: 14776.702 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: PET3D / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: O15540 |
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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: 2-3.5MM B-FABP PHOSPHATE BUFFER; 0.05% SODIUM AZIDE |
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Sample conditions | Ionic strength: 20mM POTASSIUM PHOSPHATE / pH: 7.00 / Pressure: AMBIENT / Temperature: 298.00 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: TORSION ANGLE DYNAMICS, SIMULATED ANNEALING, ENERGY MINIMIZATION Software ordinal: 1 Details: THE STRUCTURES ARE BASED ON A TOTAL OF 2490 NOE-DERIVED DISTANCE RESTRAINTS | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 300 / Conformers submitted total number: 20 |