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- PDB-3ifb: NMR STUDY OF HUMAN INTESTINAL FATTY ACID BINDING PROTEIN -

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Basic information

Entry
Database: PDB / ID: 3ifb
TitleNMR STUDY OF HUMAN INTESTINAL FATTY ACID BINDING PROTEIN
ComponentsINTESTINAL FATTY ACID BINDING PROTEIN
KeywordsLIPID BINDING PROTEIN / FATTY ACID BINDING PROTEIN / INTRACELLULAR LIPID BINDING PROTEIN / FATTY ACID BINDING / SINGLE BASE POLYMORPHISM
Function / homology
Function and homology information


intestinal lipid absorption / apical cortex / long-chain fatty acid transmembrane transporter activity / long-chain fatty acid binding / Triglyceride catabolism / microvillus / fatty acid transport / fatty acid metabolic process / fatty acid binding / nucleus / cytosol
Similarity search - Function
Fatty acid-binding protein, intestinal / Cytosolic fatty-acid binding proteins signature. / Intracellular lipid binding protein / Cytosolic fatty-acid binding / Calycin beta-barrel core domain / Lipocalin / cytosolic fatty-acid binding protein family / Lipocalin/cytosolic fatty-acid binding domain / Calycin / Lipocalin / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Fatty acid-binding protein, intestinal
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING
AuthorsZhang, F. / Luecke, C. / Baier, L.J. / Sacchettini, J.C. / Hamilton, J.A.
Citation
Journal: J.Biomol.NMR / Year: 1997
Title: Solution structure of human intestinal fatty acid binding protein: implications for ligand entry and exit.
Authors: Zhang, F. / Lucke, C. / Baier, L.J. / Sacchettini, J.C. / Hamilton, J.A.
#1: Journal: J.Biol.Chem. / Year: 1996
Title: A Polymorphism in the Human Intestinal Fatty Acid Binding Protein Alters Fatty Acid Transport Across Caco-2 Cells
Authors: Baier, L.J. / Bogardus, C. / Sacchettini, J.C.
#2: Journal: J.Clin.Invest. / Year: 1995
Title: An Amino Acid Substitution in the Human Intestinal Fatty Acid Binding Protein is Associated with Increased Fatty Acid Binding, Increased Fat Oxidation, and Insulin Resistance
Authors: Baier, L.J. / Sacchettini, J.C. / Knowler, W.C. / Eads, J. / Paolisso, G. / Tataranni, P.A. / Mochizuki, H. / Bennet, P.H. / Bogardus, C. / Prochazka, M.
#3: Journal: J.Biol.Chem. / Year: 1992
Title: Refinement of the Structure of Recombinant Rat Intestinal Fatty Acid-Binding Apoprotein at 1.2-Angstroms Resolution
Authors: Scapin, G. / Gordon, J.I. / Sacchettini, J.C.
History
DepositionOct 16, 1998Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 21, 1998Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations
Category: pdbx_struct_assembly / pdbx_struct_oper_list ...pdbx_struct_assembly / pdbx_struct_oper_list / struct_conf / struct_conf_type
Revision 1.4Dec 27, 2023Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: INTESTINAL FATTY ACID BINDING PROTEIN


Theoretical massNumber of molelcules
Total (without water)15,0981
Polymers15,0981
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 50LOWEST VIOLATION OF EXPERIMENTAL DISTANCE CONSTRAINTS
Representative

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Components

#1: Protein INTESTINAL FATTY ACID BINDING PROTEIN / I-FABP


Mass: 15098.044 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: PH 6.5, 310K, HOLO PROTEIN / Source: (gene. exp.) Homo sapiens (human) / Strain: BL21 (DE3) / Tissue: PROXIMAL SMALL INTESTINE / Cell: EPITHELIAL CELLS / Cellular location: CYTOPLASM / Gene: FABP2 / Organ: INTESTINE / Plasmid: PET-3D / Species (production host): Escherichia coli / Cellular location (production host): CYTOPLASM / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P12104

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: HMQC
NMR detailsText: SET OF 10 ENERGY-MINIMIZED NMR STRUCTURES 20MM PHOSPHATE BUFFER

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Sample preparation

Sample conditionspH: 6.5 / Temperature: 310 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 500 MHz

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Processing

NMR software
NameVersionDeveloperClassification
SYBYL6.2TRIPOS INC.refinement
DIANAstructure solution
SYBYLstructure solution
RefinementMethod: DISTANCE GEOMETRY, SIMULATED ANNEALING / Software ordinal: 1
Details: RESTRAINED SIMULATED ANNEALING AND ENERGY MINIMIZATION
NMR ensembleConformer selection criteria: LOWEST VIOLATION OF EXPERIMENTAL DISTANCE CONSTRAINTS
Conformers calculated total number: 50 / Conformers submitted total number: 10

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