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- PDB-1bwy: NMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN -

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Basic information

Entry
Database: PDB / ID: 1bwy
TitleNMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN
ComponentsPROTEIN (HEART FATTY ACID BINDING PROTEIN)
KeywordsLIPID BINDING PROTEIN / INTRACELLULAR LIPID BINDING PROTEIN / FATTY ACID BINDING / HEART MUSCLE / FATTY ACID BINDING PROTEIN
Function / homology
Function and homology information


Triglyceride catabolism / long-chain fatty acid binding / long-chain fatty acid transport / mitochondrial matrix / 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, heart
Similarity search - Component
Biological speciesBos taurus (domestic cattle)
MethodSOLUTION NMR / DISTANCE GEOMETRY, ENERGY MINIMIZATION
AuthorsLassen, D. / Luecke, C. / Kveder, M. / Mesgarzadeh, A. / Schmidt, J.M. / Specht, B. / Lezius, A. / Spener, F. / Rueterjans, H.
Citation
Journal: Eur.J.Biochem. / Year: 1995
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.
#1: Journal: Eur.J.Biochem. / Year: 1992
Title: Sequence-Specific 1H-NMR Assignment and Determination of the Secondary Structure of Bovine Heart Fatty-Acid-Binding Protein
Authors: Luecke, C. / Lassen, D. / Kreienkamp, H.-J. / Spener, F. / Rueterjans, H.
#2: Journal: J.Biol.Chem. / Year: 1992
Title: Three-Dimensional Structure of Recombinant Human Muscle Fatty-Acid Binding Protein
Authors: Zanotti, G. / Scapin, G. / Spadon, P. / Veerkamp, J.H. / Sacchettini, J.C.
History
DepositionSep 29, 1998Deposition site: BNL / Processing site: RCSB
Revision 1.0Oct 7, 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 1.4Apr 10, 2024Group: 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: PROTEIN (HEART FATTY ACID BINDING PROTEIN)


Theoretical massNumber of molelcules
Total (without water)14,6671
Polymers14,6671
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)25 / 100LOWEST VIOLATION OF EXPERIMENTAL DISTANCE CONSTRAINTS
Representative

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Components

#1: Protein PROTEIN (HEART FATTY ACID BINDING PROTEIN) / H-FABP / MAMMARY DERIVED GROWTH INHIBITOR / MDGI


Mass: 14666.694 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: PI 5.1 ISOFORM, HOLO PROTEIN / Source: (gene. exp.) Bos taurus (domestic cattle) / Strain: BL21 (DE3) PLYSS / Tissue: HEART MUSCLE / Cellular location: CYTOPLASM / Organ: HEART / Plasmid: PET-3D / Cellular location (production host): CYTOPLASM / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) PLYSS / References: UniProt: P10790

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: HMQC
NMR detailsText: SET OF 25 ENERGY-MINIMIZED NMR STRUCTURES

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Sample preparation

Sample conditionspH: 6 / Temperature: 310 K

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NMR measurement

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

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Processing

NMR software
NameVersionDeveloperClassification
SYBYL6TRIPOS INC.refinement
DIANAstructure solution
SYBYLstructure solution
RefinementMethod: DISTANCE GEOMETRY, ENERGY MINIMIZATION / Software ordinal: 1
NMR ensembleConformer selection criteria: LOWEST VIOLATION OF EXPERIMENTAL DISTANCE CONSTRAINTS
Conformers calculated total number: 100 / Conformers submitted total number: 25

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