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Yorodumi- PDB-1srj: STRUCTURE-BASED DESIGN OF SYNTHETIC AZOBENZENE LIGANDS FOR STREPT... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1srj | ||||||
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Title | STRUCTURE-BASED DESIGN OF SYNTHETIC AZOBENZENE LIGANDS FOR STREPTAVIDIN | ||||||
Components | STREPTAVIDIN | ||||||
Keywords | BIOTIN-BINDING PROTEIN | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Streptomyces avidinii (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.8 Å | ||||||
Authors | Weber, P.C. / Salemme, F.R. | ||||||
Citation | Journal: J.Am.Chem.Soc. / Year: 1994 Title: Structure-Based Design of Synthetic Azobenzene Ligands for Streptavidin Authors: Weber, P.C. / Pantoliano, M.W. / Simons, D.M. / Salemme, F.R. #1: Journal: J.Am.Chem.Soc. / Year: 1992 Title: Crystallographic and Thermodynamic Comparison of Natural and Synthetic Ligands Bound to Streptavidin Authors: Weber, P.C. / Wendoloski, J.J. / Pantoliano, M.W. / Salemme, F.R. #2: Journal: Science / Year: 1989 Title: Structural Origins of High-Affinity Biotin Binding to Streptavidin Authors: Weber, P.C. / Ohlendorf, D.H. / Wendoloski, J.J. / Salemme, F.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1srj.cif.gz | 58.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1srj.ent.gz | 43.5 KB | Display | PDB format |
PDBx/mmJSON format | 1srj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1srj_validation.pdf.gz | 507.3 KB | Display | wwPDB validaton report |
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Full document | 1srj_full_validation.pdf.gz | 516.5 KB | Display | |
Data in XML | 1srj_validation.xml.gz | 8 KB | Display | |
Data in CIF | 1srj_validation.cif.gz | 12 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sr/1srj ftp://data.pdbj.org/pub/pdb/validation_reports/sr/1srj | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 12738.730 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptomyces avidinii (bacteria) / References: UniProt: P22629 #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.38 Å3/Da / Density % sol: 48.37 % | ||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 30 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.8 Å / Num. obs: 20894 / Num. measured all: 103092 / Rmerge(I) obs: 0.079 |
-Processing
Software |
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Refinement | Resolution: 1.8→10 Å / σ(F): 3 /
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Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ/PROFFT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.177 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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