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Open data
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Basic information
| Entry | Database: PDB / ID: 1syb | ||||||
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| Title | TRANSFER OF A BETA-TURN STRUCTURE TO A NEW PROTEIN CONTEXT | ||||||
Components | STAPHYLOCOCCAL NUCLEASE | ||||||
Keywords | HYDROLASE(PHOSPHORIC DIESTER) | ||||||
| Function / homology | Function and homology informationmicrococcal nuclease / : / nucleic acid binding / extracellular region / metal ion binding / membrane Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / Resolution: 1.8 Å | ||||||
Authors | Hynes, T.R. / Kautz, R.A. / Goodman, M.A. / Gill, J.F. / Fox, R.O. | ||||||
Citation | Journal: Nature / Year: 1989Title: Transfer of a beta-turn structure to a new protein context. Authors: Hynes, T.R. / Kautz, R.A. / Goodman, M.A. / Gill, J.F. / Fox, R.O. #1: Journal: Proteins / Year: 1991Title: The Crystal Structure of Staphylococcal Nuclease Refined at 1.7 Angstroms Resolution Authors: Hynes, T.R. / Fox, R.O. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1syb.cif.gz | 42.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1syb.ent.gz | 28.9 KB | Display | PDB format |
| PDBx/mmJSON format | 1syb.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1syb_validation.pdf.gz | 448 KB | Display | wwPDB validaton report |
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| Full document | 1syb_full_validation.pdf.gz | 451.5 KB | Display | |
| Data in XML | 1syb_validation.xml.gz | 5 KB | Display | |
| Data in CIF | 1syb_validation.cif.gz | 7.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sy/1syb ftp://data.pdbj.org/pub/pdb/validation_reports/sy/1syb | HTTPS FTP |
-Related structure data
| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| Unit cell |
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| Atom site foot note | 1: CIS PROLINE - PRO 117 |
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Components
| #1: Protein | Mass: 16798.184 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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| #2: Chemical | ChemComp-CA / |
| #3: Chemical | ChemComp-THP / |
| #4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 2.21 Å3/Da / Density % sol: 44.38 % |
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| Crystal grow | *PLUS Method: otherDetails: Arnone, A., (1969) Proc.Natl.Acad.Sci.USA, 64, 420. |
-Data collection
| Reflection | *PLUS Highest resolution: 1.8 Å / Num. obs: 13418 / % possible obs: 93 % / Num. measured all: 29913 / Rmerge(I) obs: 0.023 |
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Processing
| Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Refinement | Resolution: 1.8→8 Å / Rfactor obs: 0.16 / σ(F): 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 1.8→8 Å
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| Refine LS restraints |
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| Refinement | *PLUS Rfactor obs: 0.16 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | *PLUS |
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