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- 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 | ||||||
![]() | FATTY ACID-BINDING PROTEIN | ||||||
![]() | LIPID BINDING PROTEIN / FATTY ACID-BINDING PROTEIN / LIPID TRANSPORT / I-FABP / LIPID-BINDING PROTEIN | ||||||
Function / homology | ![]() Triglyceride catabolism / intestinal lipid absorption / apical cortex / intestinal absorption / long-chain fatty acid transmembrane transporter activity / long-chain fatty acid binding / microvillus / fatty acid transport / long-chain 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 / microvillus / fatty acid transport / long-chain fatty acid transport / fatty acid metabolic process / fatty acid binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / SIMULATED ANNEALING REFINEMENT | ||||||
![]() | Hodsdon, M.E. / Cistola, D.P. | ||||||
![]() | ![]() 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: ![]() 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: ![]() 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: ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 825.3 KB | Display | ![]() |
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PDB format | ![]() | 683.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 358.7 KB | Display | ![]() |
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Full document | ![]() | 676.2 KB | Display | |
Data in XML | ![]() | 125.5 KB | Display | |
Data in CIF | ![]() | 161 KB | Display | |
Arichive directory | ![]() ![]() | 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 |