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- PDB-1eal: NMR STUDY OF ILEAL LIPID BINDING PROTEIN -

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Basic information

Entry
Database: PDB / ID: 1eal
TitleNMR STUDY OF ILEAL LIPID BINDING PROTEIN
ComponentsILEAL LIPID BINDING PROTEIN
KeywordsFATTY ACID BINDING PROTEIN / INTRACELLULAR LIPID BINDING PROTEIN / BILE ACID BINDING / ILEAL EPITHELIUM
Function / homology
Function and homology information


fatty acid transport / fatty acid binding / nucleus / membrane / 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 / Lipocalin / cytosolic fatty-acid binding protein family / Calycin beta-barrel core domain / Calycin / Lipocalin / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Biological speciesSus scrofa (pig)
MethodSOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING
AuthorsLuecke, C. / Zhang, F. / Rueterjans, H. / Hamilton, J.A. / Sacchettini, J.C.
Citation
Journal: Structure / Year: 1996
Title: Flexibility is a likely determinant of binding specificity in the case of ileal lipid binding protein.
Authors: Lucke, C. / Zhang, F. / Ruterjans, H. / Hamilton, J.A. / Sacchettini, J.C.
#1: 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.
#2: Journal: J.Biol.Chem. / Year: 1990
Title: Developmental and Structural Studies of an Intracellular Lipid Binding Protein Expressed in the Ileal Epithelium
Authors: Sacchettini, J.C. / Hauft, S.M. / Van Camp, S.L. / Cistola, D.P. / Gordon, J.I.
History
DepositionAug 28, 1996Processing site: BNL
Revision 1.0Jan 22, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _struct_ref_seq_dif.details
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: ILEAL LIPID BINDING PROTEIN


Theoretical massNumber of molelcules
Total (without water)14,0941
Polymers14,0941
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)5 / 5LOWEST VIOLATION OF EXPERIMENTAL DISTANCE CONSTRAINTS
Representative

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Components

#1: Protein ILEAL LIPID BINDING PROTEIN / GASTROTROPIN


Mass: 14093.877 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: PH 5.0, 310K, APO FORM / Source: (gene. exp.) Sus scrofa (pig) / Tissue: ILEAL EPITHELIUM / Cell line: BL21 / Organ: INTESTINE / Plasmid: PET-3D / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P10289

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111TOCSY
121NOESY
131COSY

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Sample preparation

Sample conditionspH: 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
SYBYL5.2TRIPOS ASSOCIATESrefinement
DIANAstructure solution
SYBYLstructure solution
RefinementMethod: DISTANCE GEOMETRY, SIMULATED ANNEALING / Software ordinal: 1
NMR ensembleConformer selection criteria: LOWEST VIOLATION OF EXPERIMENTAL DISTANCE CONSTRAINTS
Conformers calculated total number: 5 / Conformers submitted total number: 5

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