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- PDB-1kgl: Solution structure of cellular retinol binding protein type-I in ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1kgl | ||||||
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Title | Solution structure of cellular retinol binding protein type-I in complex with all-trans-retinol | ||||||
![]() | CELLULAR RETINOL-BINDING PROTEIN TYPE I | ||||||
![]() | LIPID BINDING PROTEIN / BETA BARREL / RETINOID CARRIER / HOLO FORM / NMR SPECTROSCOPY / 15N ISOTOPE ENRICHMENT | ||||||
Function / homology | ![]() 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 | ![]() ![]() | ||||||
Method | SOLUTION NMR / TORSION ANGLE DYNAMICS, SIMULATED ANNEALING, ENERGY MINIMIZATION | ||||||
![]() | Franzoni, L. / Luecke, C. / Perez, C. / Cavazzini, D. / Rademacher, M. / Ludwig, C. / Spisni, A. / Rossi, G.L. / Rueterjans, H. | ||||||
![]() | ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 888.7 KB | Display | ![]() |
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PDB format | ![]() | 741.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 432.3 KB | Display | ![]() |
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Full document | ![]() | 542.1 KB | Display | |
Data in XML | ![]() | 66.3 KB | Display | |
Data in CIF | ![]() | 80.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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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.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-RTL / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 1.8MM 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 |
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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 2826 NOE-DERIVED DISTANCE RESTRAINTS | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |