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- PDB-1jjx: Solution Structure of Recombinant Human Brain-type Fatty acid Bin... -

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Basic information

Entry
Database: PDB / ID: 1jjx
TitleSolution Structure of Recombinant Human Brain-type Fatty acid Binding Protein
ComponentsBRAIN-TYPE FATTY ACID BINDING PROTEIN
KeywordsLIPID BINDING PROTEIN / BETA BARREL / FATTY ACID CARRIER / 15N ISOTOPE ENRICHMENT / NMR SPECTROSCOPY
Function / homology
Function and homology information


NOTCH3 Intracellular Domain Regulates Transcription / Triglyceride catabolism / fatty acid transport / fatty acid binding / epithelial cell proliferation / nervous system development / negative regulation of cell population proliferation / lipid binding / nucleus / cytosol
Similarity search - Function
Cytosolic fatty-acid binding proteins signature. / Intracellular lipid binding protein / Cytosolic fatty-acid binding / Lipocalin / cytosolic fatty-acid binding protein family / Lipocalin/cytosolic fatty-acid binding domain / Calycin beta-barrel core domain / Calycin / Lipocalin / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Fatty acid-binding protein, brain
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / TORSION ANGLE DYNAMICS, SIMULATED ANNEALING, ENERGY MINIMIZATION
AuthorsRademacher, M. / Zimmerman, A.W. / Rueterjans, H. / Veerkamp, J.H. / Luecke, C.
Citation
Journal: Mol.Cell.Biochem. / Year: 2002
Title: Solution structure of fatty acid-binding protein from human brain.
Authors: Rademacher, M. / Zimmerman, A.W. / Ruterjans, H. / Veerkamp, J.H. / Lucke, C.
#1: Journal: J.Biol.Chem. / Year: 2000
Title: Crystal Structure and Thermodynamic Analysis of Human Brain Fatty Acid-Binding Protein
Authors: Balendiran, G.K. / Schnuetgen, F. / Scapin, G. / Boerchers, T. / Xhong, N. / Lim, K. / Godbout, R. / Spener, F. / Sacchettini, J.C.
History
DepositionJul 10, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 30, 2002Provider: repository / Type: Initial release
Revision 1.1Oct 21, 2007Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: BRAIN-TYPE FATTY ACID BINDING PROTEIN


Theoretical massNumber of molelcules
Total (without water)14,7771
Polymers14,7771
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 300target function
Representative

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Components

#1: Protein BRAIN-TYPE FATTY ACID BINDING PROTEIN / B-FABP


Mass: 14776.702 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: PET3D / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: O15540

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D TOCSY
1212D NOESY
1312D 15N-HSQC
1412D 15N-HTQC
1513D 15N-TOCSY-HSQC
1613D 15N-NOESY-HSQC

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Sample preparation

DetailsContents: 2-3.5MM B-FABP PHOSPHATE BUFFER; 0.05% SODIUM AZIDE
Sample conditionsIonic strength: 20mM POTASSIUM PHOSPHATE / pH: 7 / Pressure: AMBIENT / Temperature: 298.00 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
Discover97MSIrefinement
XwinNMR1.3structure solution
AURELIA2.5.9structure solution
DYANA1.5structure solution
RefinementMethod: TORSION ANGLE DYNAMICS, SIMULATED ANNEALING, ENERGY MINIMIZATION
Software ordinal: 1
Details: THE STRUCTURES ARE BASED ON A TOTAL OF 2490 NOE-DERIVED DISTANCE RESTRAINTS
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 300 / Conformers submitted total number: 20

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