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- PDB-1mvg: NMR solution structure of chicken Liver basic Fatty Acid Binding ... -

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Basic information

Entry
Database: PDB / ID: 1mvg
TitleNMR solution structure of chicken Liver basic Fatty Acid Binding Protein (Lb-FABP)
ComponentsLiver basic Fatty Acid Binding Protein
KeywordsTRANSPORT PROTEIN / beta-barrel / Calycin / ten antiparallel beta strands / helix-turn-helix motif / fatty acid binding protein
Function / homology
Function and homology information


fatty acid transport / fatty acid binding / nucleus / cytosol
Similarity search - Function
Lipocalin / cytosolic fatty-acid binding protein family / Cytosolic fatty-acid binding proteins signature. / Intracellular lipid binding protein / Cytosolic fatty-acid binding / Calycin beta-barrel core domain / Calycin / Lipocalin / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Fatty acid-binding protein, liver
Similarity search - Component
Biological speciesGallus gallus (chicken)
MethodSOLUTION NMR / Torsion angle Dynamics Simulated annealing Energy minimisation
AuthorsVasile, F. / Ragona, L. / Catalano, M. / Zetta, L. / Perduca, M. / Monaco, H. / Molinari, H.
CitationJournal: J.BIOMOL.NMR / Year: 2003
Title: Solution Structure of chicken Liver basic type Fatty Acid Binding Protein
Authors: Vasile, F. / Ragona, L. / Catalano, M. / Zetta, L. / Perduca, M. / Monaco, H. / Molinari, H.
History
DepositionSep 25, 2002Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 4, 2003Provider: repository / Type: Initial release
Revision 1.1Apr 28, 2008Group: 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: Liver basic Fatty Acid Binding Protein


Theoretical massNumber of molelcules
Total (without water)14,1001
Polymers14,1001
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)10 / 20structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein Liver basic Fatty Acid Binding Protein / L-FABP / Liver basic FABP / LB-FABP


Mass: 14100.177 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: purified from chicken liver / Source: (natural) Gallus gallus (chicken) / Tissue: liver / Keywords: transport, lipid-binding, acetylation / References: UniProt: P80226

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D TOCSY
1212D NOESY
131DQF-COSY
1422D TOCSY
1522D NOESY

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Sample preparation

Details
Solution-IDContentsSolvent system
11mM Liver basic Fatty Acid Binding Protein; 20mM phosphate buffer95% H2O/5% D2O
21mM Liver basic Fatty Acid Binding Protein; 20mM phosphate bufferD2O
Sample conditions
Conditions-IDIonic strengthpHPressure (kPa)Temperature (K)
120mM phosphate buffer Na 5.6 ambient 310 K
220mM phosphate buffer Na 5.6 ambient 310 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DMXBrukerDMX5001
Bruker DRXBrukerDRX5002

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR2.6Brukerprocessing
XEASY1.3.13Bartelsdata analysis
DYANA1.5Guentertrefinement
Discover1998MSIrefinement
MOLMOL2k.1Koradidata analysis
RefinementMethod: Torsion angle Dynamics Simulated annealing Energy minimisation
Software ordinal: 1
Details: The structures are based on a total of 1293 non redundant restraints, 1179 are NOE-derived distance constraints, 64 dihedral angle restarints, 50 distance restraints from hydrogen bonds
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 20 / Conformers submitted total number: 10

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