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- PDB-1bw4: THREE-DIMENSIONAL STRUCTURE IN SOLUTION OF BARWIN, A PROTEIN FROM... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1bw4 | ||||||
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Title | THREE-DIMENSIONAL STRUCTURE IN SOLUTION OF BARWIN, A PROTEIN FROM BARLEY SEED | ||||||
![]() | BARWIN, BASIC BARLEY SEED PROTEIN | ||||||
![]() | LECTIN | ||||||
Function / homology | ![]() RNA nuclease activity / defense response to fungus / carbohydrate binding / defense response to bacterium Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Poulsen, F.M. | ||||||
![]() | ![]() Title: Three-dimensional structure in solution of barwin, a protein from barley seed. Authors: Ludvigsen, S. / Poulsen, F.M. #1: ![]() 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: ![]() Title: The Secondary Structure in Solution of Barwin from Barley Seed Using 1H Nuclear Magnetic Resonance Spectroscopy Authors: Ludvigsen, S. / Poulsen, F.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 732.8 KB | Display | ![]() |
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PDB format | ![]() | 624.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Atom site foot note | 1: CIS PROLINE - PRO 15 / 2: CIS PROLINE - PRO 54 | |||||||||
NMR ensembles |
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Components
#1: Protein | Mass: 13751.166 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
Software |
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NMR software | Name: ![]() | ||||||||
NMR ensemble | Conformers submitted total number: 20 |