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Open data
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Basic information
Entry | Database: PDB / ID: 8ao0 | ||||||
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Title | Solution structure of nanoFAST/HBR-DOM2 complex | ||||||
![]() | Photoactive yellow protein | ||||||
![]() | FLUORESCENT PROTEIN / fluorogen-activating protein / FAST / nanoFAST / spatial structure / dynamics / ligand sepcificity / fluorogen / binding constatnt | ||||||
Function / homology | ![]() photoreceptor activity / phototransduction / regulation of DNA-templated transcription / identical protein binding Similarity search - Function | ||||||
Biological species | synthetic construct (others) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
![]() | Lushpa, V.A. / Goncharuk, M.V. / Goncharuk, S.A. / Baleeva, N.S. / Baranov, M.S. / Mineev, K.S. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Spatial Structure of NanoFAST in the Apo State and in Complex with its Fluorogen HBR-DOM2. Authors: Lushpa, V.A. / Baleeva, N.S. / Goncharuk, S.A. / Goncharuk, M.V. / Arseniev, A.S. / Baranov, M.S. / Mineev, K.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 685.8 KB | Display | ![]() |
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PDB format | ![]() | 578.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 510.6 KB | Display | ![]() |
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Full document | ![]() | 602.5 KB | Display | |
Data in XML | ![]() | 37.5 KB | Display | |
Data in CIF | ![]() | 59.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8ao1C C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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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: 12489.214 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) synthetic construct (others) / Gene: pyp / Production host: ![]() ![]() |
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#2: Chemical | ChemComp-O1F / ( |
Has ligand of interest | Y |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Type: solid Contents: 20 mM NaPi, 20 mM sodium chloride, 0.001 % sodium azide, 90% H2O/10% D2O Label: 15N, 13C_sample / Solvent system: 90% H2O/10% D2O | ||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: NULL mM / Label: conditions_1 / pH: 7.0 / Pressure: AMBIENT Pa / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE III / Manufacturer: Bruker / Model: AVANCE III / Field strength: 800 MHz |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 |