+Open data
-Basic information
Entry | Database: PDB / ID: 2rsc | ||||||
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Title | Solution Structure of the bombyx mori lysozyme | ||||||
Components | Lysozyme | ||||||
Keywords | HYDROLASE / LYSOZYME | ||||||
Function / homology | Function and homology information metabolic process / lysozyme / lysozyme activity / killing of cells of another organism / defense response to bacterium Similarity search - Function | ||||||
Biological species | Bombyx mori (domestic silkworm) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, DGSA-distance geometry simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Sato, M. / Tochio, N. / Aizawa, T. | ||||||
Citation | Journal: To be Published Title: Solution Structure of the Bombyx Mori LYSOZYME Authors: Sato, M. / Tochio, N. / Watanabe, S. / Kigawa, T. / Aizawa, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2rsc.cif.gz | 731.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2rsc.ent.gz | 613.6 KB | Display | PDB format |
PDBx/mmJSON format | 2rsc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2rsc_validation.pdf.gz | 453.1 KB | Display | wwPDB validaton report |
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Full document | 2rsc_full_validation.pdf.gz | 532.3 KB | Display | |
Data in XML | 2rsc_validation.xml.gz | 32.9 KB | Display | |
Data in CIF | 2rsc_validation.cif.gz | 58.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rs/2rsc ftp://data.pdbj.org/pub/pdb/validation_reports/rs/2rsc | HTTPS FTP |
-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: 13834.649 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bombyx mori (domestic silkworm) / Production host: CELL-FREE SYNTHESIS (others) / References: UniProt: P48816, lysozyme |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 20 mM sodium acetate-1, 100 mM sodium chloride-2, 0.02 % sodium azide-3, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||
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Sample |
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Sample conditions | Ionic strength: 120 / pH: 3.8 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics, DGSA-distance geometry simulated annealing Software ordinal: 1 | |||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 / Representative conformer: 1 |