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- PDB-1gh1: NMR STRUCTURES OF WHEAT NONSPECIFIC LIPID TRANSFER PROTEIN -

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Basic information

Entry
Database: PDB / ID: 1gh1
TitleNMR STRUCTURES OF WHEAT NONSPECIFIC LIPID TRANSFER PROTEIN
ComponentsNONSPECIFIC LIPID TRANSFER PROTEIN
KeywordsLIPID BINDING PROTEIN / 4-HELIX WINDING
Function / homology
Function and homology information


lipid transport / lipid binding
Similarity search - Function
Plant lipid transfer proteins signature. / Plant non-specific lipid-transfer protein/Par allergen / Plant lipid-transfer and hydrophobic proteins / Hydrophobic Seed Protein / Protease inhibitor/seed storage/LTP family / Plant lipid transfer protein / seed storage protein / trypsin-alpha amylase inhibitor domain family / Bifunctional inhibitor/plant lipid transfer protein/seed storage helical domain / Bifunctional inhibitor/plant lipid transfer protein/seed storage helical domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Non-specific lipid-transfer protein
Similarity search - Component
Biological speciesTriticum aestivum (bread wheat)
MethodSOLUTION NMR / distance geometry
AuthorsGincel, E. / Simorre, J.P. / Caille, A. / Marion, D. / Ptak, M. / Vovelle, F.
Citation
Journal: Eur.J.Biochem. / Year: 1994
Title: Three-dimensional structure in solution of a wheat lipid-transfer protein from multidimensional 1H-NMR data. A new folding for lipid carriers.
Authors: Gincel, E. / Simorre, J.P. / Caille, A. / Marion, D. / Ptak, M. / Vovelle, F.
#1: Journal: Eur.J.Biochem. / Year: 1994
Title: Three-dimensional Structure in Solution of a Wheat Lipid-transfer Protein from Multidimensional 1H-NMR Data. A New Folding for Lipid Carriers.
Authors: Gincel, E. / Simorre, J.P. / Caille, A. / Marion, D. / Ptak, M. / Vovelle, F.
History
DepositionOct 29, 2000Deposition site: RCSB / Processing site: RCSB
SupersessionNov 22, 2000ID: 1lpt
Revision 1.0Nov 22, 2000Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 15, 2017Group: Database references / Derived calculations
Category: pdbx_database_related / pdbx_struct_assembly ...pdbx_database_related / pdbx_struct_assembly / pdbx_struct_assembly_prop / pdbx_struct_oper_list
Item: _pdbx_database_related.db_name
Revision 1.4Dec 27, 2023Group: 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: NONSPECIFIC LIPID TRANSFER PROTEIN


Theoretical massNumber of molelcules
Total (without water)9,6191
Polymers9,6191
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area0 Å2
ΔGint0 kcal/mol
Surface area5370 Å2
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)15 / 50agreement with experimental NOESY spectra
RepresentativeModel #1fewest violations

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Components

#1: Protein NONSPECIFIC LIPID TRANSFER PROTEIN


Mass: 9618.860 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Triticum aestivum (bread wheat) / Organ: SEEDS / References: UniProt: P24296

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: 2D 1H-NOESY, 60-ms mixing time

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Sample preparation

DetailsContents: 4mM lipid transfer protein, 50mM acetate buffer; 90% H2O, 10% D2O
Solvent system: 90% H2O/10% D2O
Sample conditionsIonic strength: 50mM acetate buffer / pH: 5.3 / Pressure: ambient / Temperature: 308 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
UXNMRBrukerprocessing
XEASYC.Bartels (1995)data analysis
DIANAP. Guntert (1991)data analysis
X-PLOR3.1A.T. Brungerrefinement
RefinementMethod: distance geometry / Software ordinal: 1
Details: The structures are based on a total of 1142 restraints, 1086 are NOE-derived distance constraints, 56 distance restraints from hydrogen bonds.
NMR representativeSelection criteria: fewest violations
NMR ensembleConformer selection criteria: agreement with experimental NOESY spectra
Conformers calculated total number: 50 / Conformers submitted total number: 15

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