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- PDB-1bw3: THREE-DIMENSIONAL STRUCTURE IN SOLUTION OF BARWIN, A PROTEIN FROM... -

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Basic information

Entry
Database: PDB / ID: 1bw3
TitleTHREE-DIMENSIONAL STRUCTURE IN SOLUTION OF BARWIN, A PROTEIN FROM BARLEY SEED
ComponentsBARWIN, BASIC BARLEY SEED PROTEIN
KeywordsLECTIN
Function / homology
Function and homology information


RNA nuclease activity / defense response to fungus / carbohydrate binding / defense response to bacterium
Similarity search - Function
Barwin domain / Barwin, conserved site / Pathogenesis-related protein-4 / Barwin family / Barwin domain signature 1. / Barwin domain signature 2. / Barwin domain profile. / RlpA-like domain / RlpA-like domain superfamily / Barwin-like endoglucanases ...Barwin domain / Barwin, conserved site / Pathogenesis-related protein-4 / Barwin family / Barwin domain signature 1. / Barwin domain signature 2. / Barwin domain profile. / RlpA-like domain / RlpA-like domain superfamily / Barwin-like endoglucanases / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Biological speciesHordeum vulgare (barley)
MethodSOLUTION NMR
AuthorsPoulsen, F.M.
Citation
Journal: Biochemistry / Year: 1992
Title: Three-dimensional structure in solution of barwin, a protein from barley seed.
Authors: Ludvigsen, S. / Poulsen, F.M.
#1: Journal: Biochemistry / Year: 1992
Title: Primary Structure of Barwin. A Barley Seed Protein Closely Related to the C-Terminal Domain of Proteins Encoded by Wound-Induced Plant Genes
Authors: Svensson, B. / Svendsen, I. / Hojrup, P. / Roepstorff, P. / Ludvigsen, S. / Poulsen, F.M.
#2: Journal: Biochemistry / Year: 1992
Title: The Secondary Structure in Solution of Barwin from Barley Seed Using 1H Nuclear Magnetic Resonance Spectroscopy
Authors: Ludvigsen, S. / Poulsen, F.M.
History
DepositionJul 6, 1992Processing site: BNL
Revision 1.0Oct 31, 1993Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_assembly ...pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.4Nov 20, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
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: BARWIN, BASIC BARLEY SEED PROTEIN


Theoretical massNumber of molelcules
Total (without water)13,7511
Polymers13,7511
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
Atom site foot note1: CIS PROLINE - PRO 15 / 2: CIS PROLINE - PRO 54
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / -
Representative

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Components

#1: Protein BARWIN, BASIC BARLEY SEED PROTEIN


Mass: 13751.166 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Hordeum vulgare (barley) / References: UniProt: P28814
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

Software
NameClassification
X-PLORmodel building
X-PLORrefinement
X-PLORphasing
NMR softwareName: X-PLOR / Developer: BRUNGER / Classification: refinement
NMR ensembleConformers submitted total number: 20

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