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- PDB-1yrh: Crystal Structure Of Trp Repressor Binding Protein Wrba in comple... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1yrh | ||||||
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Title | Crystal Structure Of Trp Repressor Binding Protein Wrba in complex with FMN | ||||||
![]() | trp repressor binding protein WrbA | ||||||
![]() | PROTEIN BINDING / alpha-beta twisted open sheet / Structural Genomics / PSI / Protein Structure Initiative / New York SGX Research Center for Structural Genomics / NYSGXRC | ||||||
Function / homology | ![]() NADPH dehydrogenase (quinone) activity / NAD(P)H dehydrogenase (quinone) / NADH:ubiquinone reductase (non-electrogenic) activity / NAD(P)H dehydrogenase (quinone) activity / FMN binding / membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Gorman, J. / Shapiro, L. / Burley, S.K. / New York SGX Research Center for Structural Genomics (NYSGXRC) | ||||||
![]() | ![]() Title: Crystal structures of the tryptophan repressor binding protein WrbA and complexes with flavin mononucleotide. Authors: Gorman, J. / Shapiro, L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 300.1 KB | Display | ![]() |
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PDB format | ![]() | 256.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2.4 MB | Display | ![]() |
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Full document | ![]() | 2.4 MB | Display | |
Data in XML | ![]() | 58 KB | Display | |
Data in CIF | ![]() | 76.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ydgC ![]() 1zwkC ![]() 1zwlC C: citing same article ( |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Details | The biological assembly is a tetramer. There are two in the asymmetric unit: A, B, C, D form one biological unit and E, F, G, H form a second |
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Components
#1: Protein | Mass: 22900.686 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: DRA0214 / Species (production host): Escherichia coli / Production host: ![]() ![]() #2: Chemical | ChemComp-FMN / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52.9 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion / pH: 4.5 Details: 2.6M AMSULFATE, 20% GLYCEROL, pH 4.5, VAPOR DIFFUSION, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Aug 9, 2004 |
Radiation | Monochromator: DIAMOND / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9793 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→20 Å / Num. all: 32107 / Num. obs: 32107 / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 3.8 % / Biso Wilson estimate: 60.5 Å2 / Rmerge(I) obs: 0.17 / Net I/σ(I): 5.6 |
Reflection shell | Resolution: 3.1→3.21 Å / Rmerge(I) obs: 0.32 / Mean I/σ(I) obs: 4.5 / Num. unique all: 3169 / % possible all: 97 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 32.47 Å2
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Refinement step | Cycle: LAST / Resolution: 3.11→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.11→3.189 Å / Total num. of bins used: 20
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