+Open data
-Basic information
Entry | Database: PDB / ID: 2kq3 | ||||||
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Title | Solution structure of SNase140 | ||||||
Components | ThermonucleaseMicrococcal nuclease | ||||||
Keywords | HYDROLASE / Nuclease | ||||||
Function / homology | Function and homology information endonuclease activity, active with either ribo- or deoxyribonucleic acids and producing 3'-phosphomonoesters / micrococcal nuclease / nucleic acid binding Similarity search - Function | ||||||
Biological species | Staphylococcus aureus (bacteria) | ||||||
Method | SOLUTION NMR / molecular dynamics, simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Wang, M. / Feng, Y. / Yao, H. / Wang, J. | ||||||
Citation | Journal: Biochemistry / Year: 2010 Title: Importance of the C-Terminal Loop L137-S141 for the Folding and Folding Stability of Staphylococcal Nuclease Authors: Wang, M. / Feng, Y. / Yao, H. / Wang, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2kq3.cif.gz | 882.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2kq3.ent.gz | 742.4 KB | Display | PDB format |
PDBx/mmJSON format | 2kq3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kq/2kq3 ftp://data.pdbj.org/pub/pdb/validation_reports/kq/2kq3 | 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: 15914.532 Da / Num. of mol.: 1 / Fragment: residues in UNP 69-208 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Staphylococcus aureus (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: A5A523, micrococcal nuclease |
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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: 50mM [U-2H] sodium acetate-1, 250mM potassium chloride-2, 1mM EDTA-3, 0.02% sodium azide-4, 0.2mM DSS-5, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 250 / pH: 5.0 / Pressure: ambient / Temperature: 300 K |
-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: molecular dynamics, 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 |