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- PDB-2f3v: Solution structure of 1-110 fragment of staphylococcal nuclease w... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2f3v | ||||||
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Title | Solution structure of 1-110 fragment of staphylococcal nuclease with V66W mutation | ||||||
![]() | Thermonuclease | ||||||
![]() | HYDROLASE / OB-Fold | ||||||
Function / homology | ![]() endonuclease activity, active with either ribo- or deoxyribonucleic acids and producing 3'-phosphomonoesters / micrococcal nuclease / nucleic acid binding / extracellular region / membrane / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing, torsion angle dynamics | ||||||
![]() | Liu, D. / Xie, T. / Feng, Y. / Shan, L. / Ye, K. / Wang, J. | ||||||
![]() | ![]() Title: Folding stability and cooperativity of the three forms of 1-110 residues fragment of staphylococcal nuclease Authors: Xie, T. / Liu, D. / Feng, Y. / Shan, L. / Wang, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 420.5 KB | Display | ![]() |
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PDB format | ![]() | 349.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 342.3 KB | Display | ![]() |
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Full document | ![]() | 461.8 KB | Display | |
Data in XML | ![]() | 25.9 KB | Display | |
Data in CIF | ![]() | 39.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 12412.477 Da / Num. of mol.: 1 / Fragment: Residues 1-110 / Mutation: V66W Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P00644, UniProt: A5A523*PLUS, micrococcal nuclease |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: 3D 15N-separated NOESY |
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Sample preparation
Details | Contents: 2mM V66W110 fragment, 50MM ACETATE BUFFER, DSS, NAN3; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 50mM ACETATE BUFFER / pH: 4.9 / Pressure: ambient / Temperature: 298 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: simulated annealing, 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: 50 / Conformers submitted total number: 12 |