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Open data
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Basic information
Entry | Database: PDB / ID: 1nuc | ||||||
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Title | STAPHYLOCOCCAL NUCLEASE, V23C VARIANT | ||||||
![]() | STAPHYLOCOCCAL NUCLEASE | ||||||
![]() | NUCLEASE | ||||||
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 | ![]() ![]() | ||||||
![]() | Wynn, R. / Harkins, P.C. / Richards, F.M. / Fox, R.O. | ||||||
![]() | ![]() Title: Mobile unnatural amino acid side chains in the core of staphylococcal nuclease. Authors: Wynn, R. / Harkins, P.C. / Richards, F.M. / Fox, R.O. #1: ![]() Title: Interactions in Nonnative and Truncated Forms of Staphylococcal Nuclease as Indicated by Mutational Free Energy Changes Authors: Wynn, R. / Anderson, C.L. / Richards, F.M. / Fox, R.O. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 49 KB | Display | ![]() |
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PDB format | ![]() | 33.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 443.3 KB | Display | ![]() |
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Full document | ![]() | 444.8 KB | Display | |
Data in XML | ![]() | 4.6 KB | Display | |
Data in CIF | ![]() | 6.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1a2tC ![]() 1a2uC ![]() 1aexC ![]() 2nucC ![]() 3nucC ![]() 5nucC ![]() 1sncS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 16847.342 Da / Num. of mol.: 1 / Mutation: V23C Source method: isolated from a genetically manipulated source Details: PDTP, 3',5'-THYMIDINE DIPHOSPHATE / Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-CA / |
#3: Chemical | ChemComp-THP / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.09 Å3/Da / Density % sol: 41.23 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / pH: 8.15 Details: 10 MM POTASSIUM PHOSPHATE, PH = 8.15, PROTEIN CONC. = 2 MGS/ML, MPD = 21%, T = 4 C, temperature 277K | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusionDetails: Loll, P.J., (1989) Proteins Struct. Funct. Genet., 5, 183. | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 278.15 K |
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Diffraction source | Source: ![]() |
Detector | Type: MACSCIENCE / Detector: IMAGE PLATE / Date: Jan 1, 1996 / Details: COLLIMATOR |
Radiation | Monochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→6 Å / Num. obs: 9359 / % possible obs: 87.9 % / Observed criterion σ(I): 2 / Redundancy: 3.7 % / Rmerge(I) obs: 0.069 / Net I/σ(I): 10 |
Reflection shell | Resolution: 1.9→1.98 Å / Redundancy: 3 % / Rmerge(I) obs: 0.072 / Mean I/σ(I) obs: 3 / % possible all: 76.5 |
Reflection shell | *PLUS % possible obs: 76.5 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1SNC Resolution: 1.9→6 Å / σ(F): 2 /
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Refinement step | Cycle: LAST / Resolution: 1.9→6 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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