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- PDB-1ure: NMR STRUCTURE OF INTESTINAL FATTY ACID-BINDING PROTEIN COMPLEXED ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ure | ||||||
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Title | NMR STRUCTURE OF INTESTINAL FATTY ACID-BINDING PROTEIN COMPLEXED WITH PALMITATE, 20 STRUCTURES | ||||||
![]() | INTESTINAL FATTY ACID-BINDING PROTEIN | ||||||
![]() | LIPID BINDING PROTEIN / LIPID-BINDING / LIPID TRANSPORT | ||||||
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 / DISTANCE GEOMETRY WITH SIMULATED ANNEALING REFINEMENT | ||||||
![]() | Hodsdon, M.E. / Ponder, J.W. / Cistola, D.P. | ||||||
![]() | ![]() 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. #1: ![]() Title: 1H, 13C and 15N Assignments and Chemical Shift-Derived Secondary Structure of Intestinal Fatty Acid-Binding Protein Authors: Hodsdon, M.E. / Toner, J.J. / 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 Protein Authors: Sacchettini, J.C. / Gordon, J.I. #4: ![]() Title: Crystal Structure of Rat Intestinal Fatty-Acid-Binding Protein. Refinement and Analysis of the Escherichia Coli-Derived Protein with Bound Palmitate Authors: Sacchettini, J.C. / Gordon, J.I. / Banaszak, L.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 836.2 KB | Display | ![]() |
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PDB format | ![]() | 703 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 405.3 KB | Display | ![]() |
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Full document | ![]() | 646.9 KB | Display | |
Data in XML | ![]() | 85.9 KB | Display | |
Data in CIF | ![]() | 105.4 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: COMPLEXED WITH PALMITATE / Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() Strain (production host): MG1655 / References: UniProt: P02693 |
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#2: Chemical | ChemComp-PLM / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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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: 310 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: DISTANCE GEOMETRY WITH SIMULATED ANNEALING REFINEMENT Software ordinal: 1 | |||||||||
NMR ensemble | Conformer selection criteria: FINAL PENALTY FUNCTION VALUES LESS THAN 10.0 Conformers calculated total number: 26 / Conformers submitted total number: 20 |