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- PDB-1afh: LIPID TRANSFER PROTEIN FROM MAIZE SEEDLINGS, NMR, 15 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 1afh
TitleLIPID TRANSFER PROTEIN FROM MAIZE SEEDLINGS, NMR, 15 STRUCTURES
ComponentsMAIZE NONSPECIFIC LIPID TRANSFER PROTEIN
KeywordsLIPID BINDING PROTEIN / LIPID-BINDING PROTEIN / LIPID TRANSFER PROTEIN / MAIZE / MOLECULAR MODELING
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 speciesZea mays (maize)
MethodSOLUTION NMR / distance geometry
AuthorsGomar, J. / Petit, M.C. / Sodano, P. / Sy, D. / Marion, D. / Kader, J.C. / Vovelle, F. / Ptak, M.
CitationJournal: Protein Sci. / Year: 1996
Title: Solution structure and lipid binding of a nonspecific lipid transfer protein extracted from maize seeds.
Authors: Gomar, J. / Petit, M.C. / Sodano, P. / Sy, D. / Marion, D. / Kader, J.C. / Vovelle, F. / Ptak, M.
History
DepositionMar 7, 1997Processing site: BNL
Revision 1.0May 15, 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 ...Database references / Derived calculations / Other / Structure summary
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_keywords
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_keywords.text
Revision 1.4Nov 13, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: MAIZE NONSPECIFIC LIPID TRANSFER PROTEIN


Theoretical massNumber of molelcules
Total (without water)9,0621
Polymers9,0621
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)15 / 200LEAST RESTRAINT VIOLATION AND ANALYSIS OF THE RAMACHANDRAN MAPS AND ENERGETIC CRITERIA
Representative

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Components

#1: Protein MAIZE NONSPECIFIC LIPID TRANSFER PROTEIN


Mass: 9062.161 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Zea mays (maize) / Organ: SEEDS / References: UniProt: P19656
Has protein modificationY

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Experimental details

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Experiment

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

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Sample preparation

Sample conditionspH: 5.5 / Temperature: 308 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker AMX 500 / Manufacturer: Bruker / Model: AMX 500 / Field strength: 500 MHz

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
XEASYstructure solution
DIANAstructure solution
XPLORstructure solution
RefinementMethod: distance geometry / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE.
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION AND ANALYSIS OF THE RAMACHANDRAN MAPS AND ENERGETIC CRITERIA
Conformers calculated total number: 200 / Conformers submitted total number: 15

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