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Yorodumi- PDB-1jbh: Solution structure of cellular retinol binding protein type-I in ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1jbh | ||||||
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Title | Solution structure of cellular retinol binding protein type-I in the ligand-free state | ||||||
Components | CELLULAR RETINOL-BINDING PROTEIN TYPE I | ||||||
Keywords | LIPID BINDING PROTEIN / BETA BARREL / RETINOID CARRIER / APO FORM / NMR SPECTROSCOPY / 15N ISOTOPE ENRICHMENT | ||||||
Function / homology | Function and homology information regulation of granulocyte differentiation / response to benzoic acid / The canonical retinoid cycle in rods (twilight vision) / Retinoid metabolism and transport / all-trans-retinol binding / retinoic acid biosynthetic process / vitamin A metabolic process / retinal binding / response to vitamin A / retinol metabolic process ...regulation of granulocyte differentiation / response to benzoic acid / The canonical retinoid cycle in rods (twilight vision) / Retinoid metabolism and transport / all-trans-retinol binding / retinoic acid biosynthetic process / vitamin A metabolic process / retinal binding / response to vitamin A / retinol metabolic process / retinoic acid metabolic process / retinol binding / lipid homeostasis / fatty acid transport / response to retinoic acid / lipid droplet / fatty acid binding / cell body / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | SOLUTION NMR / TORSION ANGLE DYNAMICS, SIMULATED ANNEALING, ENERGY MINIMIZATION | ||||||
Authors | Franzoni, L. / Luecke, C. / Perez, C. / Cavazzini, D. / Rademacher, M. / Ludwig, C. / Spisni, A. / Rossi, G.L. / Rueterjans, H. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2002 Title: Structure and backbone dynamics of Apo- and holo-cellular retinol-binding protein in solution. Authors: Franzoni, L. / Lucke, C. / Perez, C. / Cavazzini, D. / Rademacher, M. / Ludwig, C. / Spisni, A. / Rossi, G.L. / Ruterjans, H. #1: Journal: J.Mol.Biol. / Year: 1993 Title: Crystallographic studies on a family of cellular lipophilic transport proteins Authors: Cowan, S.W. / Newcomer, M.E. / Jones, T.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jbh.cif.gz | 864.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jbh.ent.gz | 723.4 KB | Display | PDB format |
PDBx/mmJSON format | 1jbh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1jbh_validation.pdf.gz | 364.9 KB | Display | wwPDB validaton report |
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Full document | 1jbh_full_validation.pdf.gz | 490.7 KB | Display | |
Data in XML | 1jbh_validation.xml.gz | 57.2 KB | Display | |
Data in CIF | 1jbh_validation.cif.gz | 77.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jb/1jbh ftp://data.pdbj.org/pub/pdb/validation_reports/jb/1jbh | HTTPS FTP |
-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 | Mass: 15856.068 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: RBP-1 / Plasmid: PET11B / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P02696 |
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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: 1.6MM CRBP-I PHOSPHATE BUFFER; 0.05% SODIUM AZIDE |
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Sample conditions | Ionic strength: 20mM POTASSIUM PHOSPHATE / pH: 6.00 / Pressure: AMBIENT / Temperature: 298.00 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 | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz |
-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 2409 NOE-DERIVED DISTANCE RESTRAINTS | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |