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- PDB-1t8v: The NMR structure of d34a i-fabp: implications for the determinan... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1t8v | ||||||
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Title | The NMR structure of d34a i-fabp: implications for the determinants of ligand binding stoichiometry | ||||||
![]() | Fatty acid-binding protein, intestinal | ||||||
![]() | LIPID BINDING PROTEIN / fatty acid / stoichiometry | ||||||
Function / homology | ![]() Triglyceride catabolism / intestinal lipid absorption / apical cortex / intestinal absorption / long-chain fatty acid transmembrane transporter activity / long-chain fatty acid binding / microvillus / fatty acid transport / long-chain fatty acid transport / fatty acid metabolic process ...Triglyceride catabolism / intestinal lipid absorption / apical cortex / intestinal absorption / long-chain fatty acid transmembrane transporter activity / long-chain fatty acid binding / microvillus / fatty acid transport / long-chain fatty acid transport / fatty acid metabolic process / fatty acid binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing, molecular dynamics, torsion angle dynamics | ||||||
![]() | Ogbay, B. / Cistola, D.P. | ||||||
![]() | ![]() Title: THE NMR STRUCTURE OF D34A I-FABP: IMPLICATIONS FOR THE DETERMINANTS OF LIGAND BINDING STOICHIOMETRY Authors: Ogbay, B. / Cistola, D.P. #1: ![]() Title: The NMR structure of a stable and compact all-B-sheet variant of intestinal fatty acid-binding protein Authors: Cistola, D.P. / Ogbay, B. / Dekoster, G.T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 389.8 KB | Display | ![]() |
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PDB format | ![]() | 319.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 355.3 KB | Display | ![]() |
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Full document | ![]() | 587.6 KB | Display | |
Data in XML | ![]() | 79.1 KB | Display | |
Data in CIF | ![]() | 108.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-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: 14971.005 Da / Num. of mol.: 1 / Mutation: D34A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy. |
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Sample preparation
Details | Contents: 20 mM potassium phosphate, 50 mM KCl, 0.5% NaN3, 95% H2O, 5% D2O Solvent system: 95% H2O/5% D2O |
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Sample conditions | Ionic strength: 50mM KCl / pH: 7.2 / Temperature: 298 K |
-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: distance geometry, simulated annealing, molecular dynamics, torsion angle dynamics Software ordinal: 1 Details: the structures are based on a total of 3471 NOE-derived restraints and 80 dihedral angle restraints. | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 20 / Conformers submitted total number: 10 |