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Yorodumi- PDB-1x60: Solution structure of the peptidoglycan binding domain of B. subt... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1x60 | ||||||
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Title | Solution structure of the peptidoglycan binding domain of B. subtilis cell wall lytic enzyme CwlC | ||||||
Components | Sporulation-specific N-acetylmuramoyl-L-alanine amidase | ||||||
Keywords | HYDROLASE / CwlC / CwlCr / peptidoglycan / cell wall lytic amidase / tandem repeats | ||||||
Function / homology | Function and homology information N-acetylmuramoyl-L-alanine amidase / establishment of competence for transformation / N-acetylmuramoyl-L-alanine amidase activity / peptidoglycan binding / cell wall / sporulation resulting in formation of a cellular spore / peptidoglycan catabolic process / cell wall organization / outer membrane-bounded periplasmic space / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | Bacillus subtilis (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Mishima, M. / Shida, T. / Yabuki, K. / Kato, K. / Sekiguchi, J. / Kojima, C. | ||||||
Citation | Journal: Biochemistry / Year: 2005 Title: Solution Structure of the Peptidoglycan Binding Domain of Bacillus subtilis Cell Wall Lytic Enzyme CwlC: Characterization of the Sporulation-Related Repeats by NMR(,) Authors: Mishima, M. / Shida, T. / Yabuki, K. / Kato, K. / Sekiguchi, J. / Kojima, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1x60.cif.gz | 678.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1x60.ent.gz | 594.5 KB | Display | PDB format |
PDBx/mmJSON format | 1x60.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/x6/1x60 ftp://data.pdbj.org/pub/pdb/validation_reports/x6/1x60 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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NMR ensembles |
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-Components
#1: Protein | Mass: 8262.405 Da / Num. of mol.: 1 / Fragment: residues 1-79 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus subtilis (bacteria) / Plasmid: pQE30 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 References: UniProt: Q06320, N-acetylmuramoyl-L-alanine amidase |
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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 conditions | Ionic strength: 70mM / pH: 6.9 / Pressure: ambient / Temperature: 303 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: 30 |