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Yorodumi- PDB-1k85: Solution structure of the fibronectin type III domain from Bacill... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1k85 | ||||||
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Title | Solution structure of the fibronectin type III domain from Bacillus circulans WL-12 Chitinase A1. | ||||||
Components | CHITINASE A1 | ||||||
Keywords | HYDROLASE / fibronectin type III domain / chitinase / chitin binding domain / carbohydrase / horizontal gene transfer | ||||||
Function / homology | Function and homology information chitinase / chitinase activity / chitin catabolic process / chitin binding / polysaccharide catabolic process / carbohydrate binding / extracellular region Similarity search - Function | ||||||
Biological species | Bacillus circulans (bacteria) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Jee, J.G. / Ikegami, T. / Hashimoto, M. / Kawabata, T. / Ikeguchi, M. / Watanabe, T. / Shirakawa, M. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2002 Title: Solution Structure of the Fibronectin Type III Domain from Bacillus circulans WL-12 Chitinase A1 Authors: Jee, J.G. / Ikegami, T. / Hashimoto, M. / Kawabata, T. / Ikeguchi, M. / Watanabe, T. / Shirakawa, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1k85.cif.gz | 686.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1k85.ent.gz | 599.9 KB | Display | PDB format |
PDBx/mmJSON format | 1k85.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/k8/1k85 ftp://data.pdbj.org/pub/pdb/validation_reports/k8/1k85 | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 8695.429 Da / Num. of mol.: 1 / Fragment: FIBRONECTIN TYPE-III Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus circulans (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: P20533, chitinase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: ARIA method was used |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 50mM KCl / pH: 6.5 / Pressure: ambient / Temperature: 310 K | ||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | ||||||||||||||||||||
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Radiation wavelength | Relative weight: 1 | ||||||||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 150 / Conformers submitted total number: 30 |