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- PDB-2flj: Fatty acid binding protein from locust flight muscle in complex w... -

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Basic information

Entry
Database: PDB / ID: 2flj
TitleFatty acid binding protein from locust flight muscle in complex with oleate
ComponentsFatty acid-binding protein
KeywordsLIPID BINDING PROTEIN / fatty acid carrier / intracellular lipid binding protein / invertebrate FABP / protein-ligand complex
Function / homology
Function and homology information


lipid binding / cytoplasm
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
OLEIC ACID / Fatty acid-binding protein, muscle
Similarity search - Component
Biological speciesLocusta migratoria (migratory locust)
MethodSOLUTION NMR / restrained molecular dynamics
AuthorsLuecke, C. / Qiao, Y. / van Moerkerk, H.T.B. / Veerkamp, J.H. / Hamilton, J.A.
CitationJournal: Biochemistry / Year: 2006
Title: Fatty-acid-binding protein from the flight muscle of Locusta migratoria: evolutionary variations in fatty acid binding.
Authors: Lucke, C. / Qiao, Y. / van Moerkerk, H.T. / Veerkamp, J.H. / Hamilton, J.A.
History
DepositionJan 6, 2006Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 23, 2006Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 9, 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 / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4May 29, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond
Remark 600HETEROGEN Potassium oleate, C18H33O2KA, a potassium salt of oleic acid was used in the experiments

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Fatty acid-binding protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)15,3702
Polymers15,0871
Non-polymers2821
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)25 / 26last MD steps
RepresentativeModel #25last molecular dynamics conformer

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Components

#1: Protein Fatty acid-binding protein / LM-FABP


Mass: 15087.383 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Locusta migratoria (migratory locust) / Plasmid: pET-3d / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P41509
#2: Chemical ChemComp-OLA / OLEIC ACID


Mass: 282.461 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C18H34O2

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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 1H-13C HSQC
1413D 13C-separated NOESY

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Sample preparation

DetailsContents: 2mM Lm-FABP complexed with U-13C potassium oleate, 20 mM Phosphate buffer, 95% H2O, 5% D2O
Solvent system: 95% H2O/5% D2O
Sample conditionsIonic strength: 20mM phosphate buffer / pH: 5.5 / Pressure: ambient / Temperature: 308 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 500 MHz

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR2.6collection
AURELIA2.5.9data analysis
Discover2000ACCELRYS INC.structure solution
Discover2000ACCELRYS INC.refinement
RefinementMethod: restrained molecular dynamics / Software ordinal: 1
NMR representativeSelection criteria: last molecular dynamics conformer
NMR ensembleConformer selection criteria: last MD steps / Conformers calculated total number: 26 / Conformers submitted total number: 25

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