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- PDB-2mm3: Solution NMR structure of the ternary complex of human ileal bile... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2mm3 | ||||||
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Title | Solution NMR structure of the ternary complex of human ileal bile acid-binding protein with glycocholate and glycochenodeoxycholate | ||||||
![]() | Gastrotropin | ||||||
![]() | LIPID BINDING PROTEIN / lipid-binding protein / orthogonal beta sheets / positive binding cooperativity / site-selectivity / enterohepatic circulation | ||||||
Function / homology | ![]() NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis / Triglyceride catabolism / fatty acid transport / Recycling of bile acids and salts / fatty acid binding / lipid metabolic process / negative regulation of cell population proliferation / lipid binding / membrane / nucleus ...NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis / Triglyceride catabolism / fatty acid transport / Recycling of bile acids and salts / fatty acid binding / lipid metabolic process / negative regulation of cell population proliferation / lipid binding / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing, torsion angle dynamics | ||||||
Model details | closest to the average, model9 | ||||||
![]() | Horvath, G. / Egyed, O. / Bencsura, A. / Simon, A. / Tochtrop, G.P. / DeKoster, G.T. / Covey, D.F. / Cistola, D.P. / Toke, O. | ||||||
![]() | ![]() Title: Structural determinants of ligand binding in the ternary complex of human ileal bile acid binding protein with glycocholate and glycochenodeoxycholate obtained from solution NMR Authors: Horvath, G. / Bencsura, A. / Simon, A. / Tochtrop, G.P. / DeKoster, G.T. / Covey, D.F. / Cistola, D.P. / Toke, O. #1: Journal: Biochemistry / Year: 2006 Title: Determinants of cooperativity and site selectivity in human ileal bile acid binding protein. Authors: Toke, O. / Monsey, J.D. / DeKoster, G.T. / Tochtrop, G.P. / Tang, C. / Cistola, D.P. #2: Journal: J.Am.Chem.Soc. / Year: 2004 Title: A single hydroxyl group governs ligand site selectivity in human ileal bile acid binding protein. Authors: Tochtrop, G.P. / DeKoster, G.T. / Covey, D.F. / Cistola, D.P. #3: Journal: Biochemistry / Year: 2007 Title: Kinetic mechanism of ligand binding in human ileal bile acid binding protein as determined by stopped-flow fluorescence analysis. Authors: Toke, O. / Monsey, J.D. / Cistola, D.P. #4: Journal: Biochemistry / Year: 2012 Title: Internal motions and exchange processes in human ileal bile acid binding protein as studied by backbone (15)N nuclear magnetic resonance spectroscopy. Authors: Horvath, G. / Kiraly, P. / Tarkanyi, G. / Toke, O. #5: ![]() Title: Internal motions and exchange processes in human ileal bile acid binding protein as studied by backbone (15)N nuclear magnetic resonance spectroscopy Authors: Horvath, G. / Kiraly, P. / Tarkanyi, G. / Toke, O. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 457.3 KB | Display | ![]() |
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PDB format | ![]() | 390.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 666.3 KB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 131.4 KB | Display | |
Data in CIF | ![]() | 94.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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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: 14258.038 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-GCH / |
#3: Chemical | ChemComp-CHO / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
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Sample conditions | Ionic strength: 70 / pH: 6.3 / Pressure: ambient / Temperature: 293 K |
-NMR measurement
NMR spectrometer | Type: Varian Varian NMR System / Manufacturer: Varian / Model: Varian NMR System / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing, torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 / Representative conformer: 9 |