+Open data
-Basic information
Entry | Database: PDB / ID: 2rst | ||||||
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Title | NMR structure of the C-terminal domain of EW29 | ||||||
Components | 29-kDa galactose-binding lectin | ||||||
Keywords | SUGAR BINDING PROTEIN / R-type lectin | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Lumbricus terrestris (common earthworm) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Hemmi, H. | ||||||
Citation | Journal: Febs J. / Year: 2013 Title: NMR structure and dynamics of the C-terminal domain of R-type lectin from the earthworm Lumbricus terrestris Authors: Hemmi, H. / Kuno, A. / Hirabayashi, J. #1: Journal: J.Biomol.Nmr / Year: 2004 Title: (1)H, (13)C, and (15)N chemical shift assignment of the C-terminal 15 kDa domain of a novel galactose-binding protein from the earthworm Lumbricus terrestris Authors: Hemmi, H. / Kuno, A. / Ito, S. / Suzuki, R. / Kaneko, S. / Hasegawa, T. / Hirabayashi, J. / Kasai, K. #2: Journal: Febs J. / Year: 2009 Title: NMR studies on the interaction of sugars with the C-terminal domain of an R-type lectin from the earthworm Lumbricus terrestris Authors: Hemmi, H. / Kuno, A. / Ito, S. / Suzuki, R. / Hasegawa, T. / Hirabayashi, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2rst.cif.gz | 811 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2rst.ent.gz | 681.8 KB | Display | PDB format |
PDBx/mmJSON format | 2rst.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rs/2rst ftp://data.pdbj.org/pub/pdb/validation_reports/rs/2rst | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 14877.745 Da / Num. of mol.: 1 / Fragment: C-terminal domain, UNP residues 130-260 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Lumbricus terrestris (common earthworm) Production host: Escherichia coli (E. coli) / References: UniProt: O96048 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | pH: 6.1 / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 / Representative conformer: 1 |