[English] 日本語
![](img/lk-miru.gif)
- PDB-1nti: RDC-refined NMR structure of bovine Acyl-coenzyme A Binding Prote... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1nti | ||||||
---|---|---|---|---|---|---|---|
Title | RDC-refined NMR structure of bovine Acyl-coenzyme A Binding Protein, ACBP | ||||||
![]() | Acyl-CoA-binding protein![]() | ||||||
![]() | LIPID BINDING PROTEIN / four-helix-bundle / ![]() | ||||||
Function / homology | ![]() Mitochondrial Fatty Acid Beta-Oxidation / fatty-acyl-CoA binding / fatty acid metabolic process / ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Lerche, M.H. / Kragelund, B.B. / Redfield, C. / Poulsen, F.M. | ||||||
![]() | ![]() Title: Subtle structural response to ligand binding revealed by residual dipolar coupling refined NMR structures of acyl coenzyme A binding protein Authors: Lerche, M.H. / Kragelund, B.B. / Redfield, C. / Poulsen, F.M. #1: ![]() Title: The three-dimensional structure of acyl-coenzyme A binding protein from bovine liver: structural refinement using heteronuclear multidimensional NMR spectroscopy. Authors: Andersen, K.V. / Poulsen, F.M. #2: ![]() Title: Three-dimensional structure of the complex between acyl-coenzyme A binding protein and palmitoyl-coenzyme A. Authors: Kragelund, B.B. / Andersen, K.V. / Madsen, J.C. / Knudsen, J. / Poulsen, F.M. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 598.8 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 512.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein | ![]() Mass: 9931.289 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||
NMR details | Text: refinement of earlier pdb deposit, 2ABD, see entry for detail. NOE and dihedral angle constraints obtained from this entry. Residual dipolar couplings added as additional restraints |
-
Sample preparation
Details |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Sample conditions | Ionic strength: no salt added / pH: 6.5 / Pressure: ambient / Temperature: 310 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
|
-
Processing
NMR software | Name: ![]() |
---|---|
Refinement | Method: ![]() ![]() |
NMR representative | Selection criteria: lowest energy |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |