[English] 日本語
Yorodumi- PDB-1nvl: RDC-refined NMR structure of bovine Acyl-coenzyme A Binding Prote... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1nvl | ||||||
---|---|---|---|---|---|---|---|
Title | RDC-refined NMR structure of bovine Acyl-coenzyme A Binding Protein, ACBP, in complex with palmitoyl-coenzyme A | ||||||
Components | Acyl-CoA-binding protein | ||||||
Keywords | LIGAND BINDING PROTEIN / 4-alpha-helix bundle / protein-ligand complex / palmitoyl-coenzyme A | ||||||
Function / homology | Function and homology information Mitochondrial Fatty Acid Beta-Oxidation / fatty-acyl-CoA binding / fatty acid metabolic process / Golgi apparatus / endoplasmic reticulum Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | SOLUTION NMR / SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS IN FULL CHARMM FORCE FIELD | ||||||
Authors | Lerche, M.H. / Kragelund, B.B. / Redfield, C. / Poulsen, F.M. | ||||||
Citation | Journal: To be Published / Year: 2003 Title: RDC-refined NMR structure of bovine Acyl-coenzyme A Binding Protein, ACBP, in complex with palmitoyl-coenzyme A Authors: Lerche, M.H. / Kragelund, B.B. / Redfield, C. / Poulsen, F.M. #1: Journal: J.Mol.Biol. / Year: 1993 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. #2: Journal: J.Biomol.NMR / Year: 1993 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. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1nvl.cif.gz | 660.4 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1nvl.ent.gz | 560.7 KB | Display | PDB format |
PDBx/mmJSON format | 1nvl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nv/1nvl ftp://data.pdbj.org/pub/pdb/validation_reports/nv/1nvl | 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.) Bos taurus (cattle) / Gene: ACBP / Plasmid: pET-3a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P07107 |
---|---|
#2: Chemical | ChemComp-COA / |
#3: Chemical | ChemComp-PLM / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||
NMR details | Text: REFINEMENT OF EARLIER PDB DEPOSIT, 1ACA, SEE ENTRY FOR DETAILS. NOE AND DIHEDRAL ANGLE CONSTRAINTS OBTAINED AND MODIFIED FROM THIS ENTRY. RESIDUAL DIPOLAR COUPLINGS ADDED AS ADDITIONAL RESTRAINTS. |
-Sample preparation
Details |
| |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample conditions |
|
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
|
-Processing
NMR software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS IN FULL CHARMM FORCE FIELD Software ordinal: 1 | ||||||||||||||||||||
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 |