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- PDB-1o1v: Human Ileal Lipid-Binding Protein (ILBP) in Complex with Cholyltaurine -

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Basic information

Entry
Database: PDB / ID: 1o1v
TitleHuman Ileal Lipid-Binding Protein (ILBP) in Complex with Cholyltaurine
ComponentsGastrotropin
KeywordsLIPID BINDING PROTEIN / BETA CLAM STRUCTURE
Function / homology
Function and homology information


NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis / Triglyceride catabolism / fatty acid transport / Recycling of bile acids and salts / fatty acid binding / lipid metabolic process / negative regulation of cell population proliferation / lipid binding / nucleus / membrane ...NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis / Triglyceride catabolism / fatty acid transport / Recycling of bile acids and salts / fatty acid binding / lipid metabolic process / negative regulation of cell population proliferation / lipid binding / nucleus / membrane / cytosol / cytoplasm
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
TAUROCHOLIC ACID / Gastrotropin
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / distance geometry (DIANA), molecular dynamics (SYBYL), energy minimization (SYBYL)
AuthorsKurz, M. / Brachvogel, V. / Matter, H. / Stengelin, S. / Thuering, H. / Kramer, W.
CitationJournal: Proteins / Year: 2003
Title: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures.
Authors: Kurz, M. / Brachvogel, V. / Matter, H. / Stengelin, S. / Thuering, H. / Kramer, W.
History
DepositionFeb 10, 2003Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 18, 2003Provider: repository / Type: Initial release
Revision 1.1Apr 26, 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 / 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_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Dec 27, 2023Group: 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: Gastrotropin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)14,7742
Polymers14,2581
Non-polymers5161
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 / 100lowest intermolecular restraint violation, DIANA target function
Representative

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Components

#1: Protein Gastrotropin / GT / Ileal lipid-binding protein / ILBP / Intestinal 15 kDa protein / I-15P / Intestinal bile acid- ...GT / Ileal lipid-binding protein / ILBP / Intestinal 15 kDa protein / I-15P / Intestinal bile acid-binding protein / I-BABP


Mass: 14258.038 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FABP6 OR ILLBP OR ILBP / Plasmid: pHUGA1 / Production host: Escherichia coli (E. coli) / References: UniProt: P51161
#2: Chemical ChemComp-TCH / TAUROCHOLIC ACID


Mass: 515.703 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C26H45NO7S

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D-NOESY
1212D DQF-COSY
1312D-TOCSY
1422D 1H-15N HSQC
1523D-NOESY-HMQC
1623D-TOCSY-HMQC
1733D HNCA
1833D HNCO
1933D-HCC(CO)NH-TOCSY
11033D (H)CCH-COSY

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Sample preparation

Details
Solution-IDContentsSolvent system
1unlabeledH2O
2uniform 15N labeledH2O
3uniform 15N/13C labeledH2O
Sample conditionsIonic strength: 50 mM KH2PO4 / pH: 6 / Pressure: ambient / Temperature: 305 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

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

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR2.6Brukerprocessing
AURELIA2.7.5Neidig, K.P.data analysis
Sybyl-TRIAD6.7TRIPOSrefinement
RefinementMethod: distance geometry (DIANA), molecular dynamics (SYBYL), energy minimization (SYBYL)
Software ordinal: 1
Details: DIANA, MD, EM, structure based on 1832 nontrivial NOE distances from 2D-NOESY incl. 40 intermolecular distances.
NMR ensembleConformer selection criteria: lowest intermolecular restraint violation, DIANA target function
Conformers calculated total number: 100 / Conformers submitted total number: 10

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