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Yorodumi- PDB-1ael: NMR STRUCTURE OF APO INTESTINAL FATTY ACID-BINDING PROTEIN, 20 ST... -
+Open data
-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 information Triglyceride catabolism / intestinal lipid absorption / apical cortex / intestinal absorption / long-chain fatty acid transmembrane transporter activity / long-chain fatty acid binding / long-chain fatty acid transport / microvillus / fatty acid transport / fatty acid metabolic process ...Triglyceride catabolism / intestinal lipid absorption / apical cortex / intestinal absorption / long-chain fatty acid transmembrane transporter activity / long-chain fatty acid binding / long-chain fatty acid transport / microvillus / fatty acid transport / fatty acid metabolic process / fatty acid binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | SOLUTION NMR / SIMULATED ANNEALING REFINEMENT | ||||||
Authors | Hodsdon, M.E. / Cistola, D.P. | ||||||
Citation | Journal: Biochemistry / Year: 1997 Title: 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: 1996 Title: 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: 1993 Title: 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: 1993 Title: 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: 1992 Title: 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: MolmilJmol/JSmol |
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-Downloads & links
-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
-Assembly
Deposited unit |
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1 |
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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.) Rattus norvegicus (Norway rat) / Cell: SMALL INTESTINAL ENTEROCYTE / Plasmid: PMON5840-I-FABP / Species (production host): Escherichia coli Production host: Escherichia coli str. K-12 substr. MG1655 (bacteria) 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. |
-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 |