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- PDB-1be2: LIPID TRANSFER PROTEIN COMPLEXED WITH PALMITATE, NMR, 10 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 1be2
TitleLIPID TRANSFER PROTEIN COMPLEXED WITH PALMITATE, NMR, 10 STRUCTURES
ComponentsLIPID TRANSFER PROTEIN
KeywordsLIPID TRANSPORT / LIPID TRANSFER PROTEIN / PALMITATE
Function / homology
Function and homology information


lipid transport / lipid binding / membrane
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
PALMITIC ACID / Non-specific lipid-transfer protein 1
Similarity search - Component
Biological speciesHordeum vulgare (barley)
MethodSOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING
AuthorsLerche, M.H. / Poulsen, F.M.
Citation
Journal: Protein Sci. / Year: 1998
Title: Solution structure of barley lipid transfer protein complexed with palmitate. Two different binding modes of palmitate in the homologous maize and barley nonspecific lipid transfer proteins.
Authors: Lerche, M.H. / Poulsen, F.M.
#1: Journal: Structure / Year: 1997
Title: Barley Lipid-Transfer Protein Complexed with Palmitoyl Coa: The Structure Reveals a Hydrophobic Binding Site that Can Expand to Fit Both Large and Small Lipid-Like Ligands
Authors: Lerche, M.H. / Kragelund, B.B. / Bech, L.M. / Poulsen, F.M.
#2: Journal: Protein Sci. / Year: 1996
Title: Structure in Solution of a Four-Helix Lipid Binding Protein
Authors: Heinemann, B. / Andersen, K.V. / Nielsen, P.R. / Bech, L.M. / Poulsen, F.M.
#3: Journal: Structure / Year: 1995
Title: High-Resolution Crystal Structure of the Non-Specific Lipid-Transfer Protein from Maize Seedlings
Authors: Shin, D.H. / Lee, J.Y. / Hwang, K.Y. / Kim, K.K. / Suh, S.W.
History
DepositionMay 19, 1998Processing site: BNL
Revision 1.0Dec 2, 1998Provider: 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: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / 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_database_status.process_site / _pdbx_nmr_software.name / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: LIPID TRANSFER PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)9,9612
Polymers9,7051
Non-polymers2561
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 / 40LOWEST TOTAL ENERGY
Representative

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Components

#1: Protein LIPID TRANSFER PROTEIN / LTP


Mass: 9704.965 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Hordeum vulgare (barley) / Organ: SEEDS / References: UniProt: P07597
#2: Chemical ChemComp-PLM / PALMITIC ACID


Mass: 256.424 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C16H32O2

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111DQF-COSY
121TOCSY
131NOESY
141HSQC
151HSQC-NOE

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Sample preparation

Sample conditionspH: 7.2 / Temperature: 310 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker AMX600 / Manufacturer: Bruker / Model: AMX600 / Field strength: 600 MHz

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Processing

Software
NameVersionClassification
X-PLOR3.8model building
X-PLOR3.8refinement
X-PLOR3.8phasing
NMR software
NameVersionDeveloperClassification
X-PLOR3.8BRUNGERrefinement
Prontostructure solution
X-PLOR3.8structure solution
RefinementMethod: DISTANCE GEOMETRY, SIMULATED ANNEALING / Software ordinal: 1
NMR ensembleConformer selection criteria: LOWEST TOTAL ENERGY / Conformers calculated total number: 40 / Conformers submitted total number: 10

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