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Open data
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Basic information
Entry | Database: PDB / ID: 1eal | ||||||
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Title | NMR STUDY OF ILEAL LIPID BINDING PROTEIN | ||||||
![]() | ILEAL LIPID BINDING PROTEIN | ||||||
![]() | FATTY ACID BINDING PROTEIN / INTRACELLULAR LIPID BINDING PROTEIN / BILE ACID BINDING / ILEAL EPITHELIUM | ||||||
Function / homology | ![]() fatty acid transport / fatty acid binding / membrane / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING | ||||||
![]() | Luecke, C. / Zhang, F. / Rueterjans, H. / Hamilton, J.A. / Sacchettini, J.C. | ||||||
![]() | ![]() Title: Flexibility is a likely determinant of binding specificity in the case of ileal lipid binding protein. Authors: Lucke, C. / Zhang, F. / Ruterjans, H. / Hamilton, J.A. / Sacchettini, J.C. #1: ![]() Title: Three-Dimensional Structure of Bovine Heart Fatty-Acid-Binding Protein with Bound Palmitic Acid, Determined by Multidimensional NMR Spectroscopy Authors: Lassen, D. / Lucke, C. / Kveder, M. / Mesgarzadeh, A. / Schmidt, J.M. / Specht, B. / Lezius, A. / Spener, F. / Ruterjans, H. #2: ![]() Title: Developmental and Structural Studies of an Intracellular Lipid Binding Protein Expressed in the Ileal Epithelium Authors: Sacchettini, J.C. / Hauft, S.M. / Van Camp, S.L. / Cistola, D.P. / Gordon, J.I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 201.4 KB | Display | ![]() |
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PDB format | ![]() | 163.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 357.3 KB | Display | ![]() |
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Full document | ![]() | 381.1 KB | Display | |
Data in XML | ![]() | 11.4 KB | Display | |
Data in CIF | ![]() | 18.6 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: 14093.877 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: PH 5.0, 310K, APO FORM / Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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Sample preparation
Sample conditions | pH: 5.0 / Temperature: 310 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 500 MHz |
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Processing
NMR software |
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Refinement | Method: DISTANCE GEOMETRY, SIMULATED ANNEALING / Software ordinal: 1 | ||||||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST VIOLATION OF EXPERIMENTAL DISTANCE CONSTRAINTS Conformers calculated total number: 5 / Conformers submitted total number: 5 |