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Yorodumi- PDB-1nti: RDC-refined NMR structure of bovine Acyl-coenzyme A Binding Prote... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1nti | ||||||
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Title | RDC-refined NMR structure of bovine Acyl-coenzyme A Binding Protein, ACBP | ||||||
Components | Acyl-CoA-binding protein | ||||||
Keywords | LIPID BINDING PROTEIN / four-helix-bundle / ACBP family | ||||||
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, molecular dynamics | ||||||
Authors | Lerche, M.H. / Kragelund, B.B. / Redfield, C. / Poulsen, F.M. | ||||||
Citation | Journal: To be Published 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: 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. #2: 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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1nti.cif.gz | 598.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1nti.ent.gz | 512.6 KB | Display | PDB format |
PDBx/mmJSON format | 1nti.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1nti_validation.pdf.gz | 354.6 KB | Display | wwPDB validaton report |
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Full document | 1nti_full_validation.pdf.gz | 513.3 KB | Display | |
Data in XML | 1nti_validation.xml.gz | 36 KB | Display | |
Data in CIF | 1nti_validation.cif.gz | 57.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nt/1nti ftp://data.pdbj.org/pub/pdb/validation_reports/nt/1nti | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-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) / Production host: Escherichia coli (E. coli) / References: UniProt: P07107 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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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 |
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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 | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software | Name: X-PLOR / Version: modified 3.8 / Classification: refinement |
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Refinement | Method: simulated annealing, molecular dynamics / 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 |