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Yorodumi- PDB-1ael: NMR STRUCTURE OF APO INTESTINAL FATTY ACID-BINDING PROTEIN, 20 ST... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 1ael | ||||||
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| Title | NMR STRUCTURE OF APO INTESTINAL FATTY ACID-BINDING PROTEIN, 20 STRUCTURES | ||||||
Components | FATTY ACID-BINDING PROTEIN | ||||||
Keywords | LIPID BINDING PROTEIN / FATTY ACID-BINDING PROTEIN / LIPID TRANSPORT / I-FABP / LIPID-BINDING PROTEIN | ||||||
| Function / homology | Function and homology informationTriglyceride catabolism / intestinal lipid absorption / apical cortex / intestinal absorption / long-chain fatty acid transmembrane transporter activity / long-chain fatty acid binding / microvillus / long-chain fatty acid transport / fatty acid transport / fatty acid binding ...Triglyceride catabolism / intestinal lipid absorption / apical cortex / intestinal absorption / long-chain fatty acid transmembrane transporter activity / long-chain fatty acid binding / microvillus / long-chain fatty acid transport / fatty acid transport / fatty acid binding / fatty acid metabolic process / nucleus / cytosol Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | SOLUTION NMR / SIMULATED ANNEALING REFINEMENT | ||||||
Authors | Hodsdon, M.E. / Cistola, D.P. | ||||||
Citation | Journal: Biochemistry / Year: 1997Title: Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange. Authors: Hodsdon, M.E. / Cistola, D.P. #1: Journal: J.Mol.Biol. / Year: 1996Title: The NMR Solution Structure of Intestinal Fatty Acid-Binding Protein Complexed with Palmitate: Application of a Novel Distance Geometry Algorithm Authors: Hodsdon, M.E. / Ponder, J.W. / Cistola, D.P. #2: Journal: Adv.Protein Chem. / Year: 1993Title: Lipid Binding Proteins: A Family of Fatty Acid and Retinoid Transport Proteins Authors: Banaszak, L. / Winter, N. / Xu, Z. / Bernlohr, D.A. / Cowan, S. / Jones, T.A. #3: Journal: J.Biol.Chem. / Year: 1993Title: Rat Intestinal Fatty Acid Binding Protein. A Model System for Analyzing the Forces that Can Bind Fatty Acids to Proteins Authors: Sacchettini, J.C. / Gordon, J.I. #4: Journal: J.Biol.Chem. / Year: 1992Title: Refinement of the Structure of Recombinant Rat Intestinal Fatty Acid-Binding Apoprotein at 1.2-A Resolution Authors: Scapin, G. / Gordon, J.I. / Sacchettini, J.C. | ||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1ael.cif.gz | 825.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1ael.ent.gz | 683.2 KB | Display | PDB format |
| PDBx/mmJSON format | 1ael.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1ael_validation.pdf.gz | 358.7 KB | Display | wwPDB validaton report |
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| Full document | 1ael_full_validation.pdf.gz | 676.2 KB | Display | |
| Data in XML | 1ael_validation.xml.gz | 125.5 KB | Display | |
| Data in CIF | 1ael_validation.cif.gz | 161 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ae/1ael ftp://data.pdbj.org/pub/pdb/validation_reports/ae/1ael | HTTPS FTP |
-Related structure data
| 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: 15015.015 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: INTESTINAL / Source: (gene. exp.) ![]() Production host: ![]() Strain (production host): MG1655 / References: UniProt: P02693 |
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-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR |
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| NMR experiment | Type: 2-D 1H-HOMONUCLEAR NOESY |
| NMR details | Text: LIMITS ON SECONDARY STRUCTURE ELEMENTS WERE DEFINED BY THE PROTON-CARBON CONSENSUS CHEMICAL SHIFT INDEX. |
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Sample preparation
| Sample conditions | pH: 7.2 / Temperature: 306 K |
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| Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
| NMR spectrometer | Type: Varian UNITY / Manufacturer: Varian / Model: UNITY / Field strength: 500 MHz |
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Processing
| NMR software |
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| Refinement | Method: SIMULATED ANNEALING REFINEMENT / Software ordinal: 1 | |||||||||
| NMR ensemble | Conformer selection criteria: FINAL PENALTY FUNCTION VALUES LESS THAN 10.0 Conformers calculated total number: 21 / Conformers submitted total number: 20 |
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