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- PDB-6pq2: Structural Basis for Client Recognition and Activity of Hsp40 Cha... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6pq2 | ||||||
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Title | Structural Basis for Client Recognition and Activity of Hsp40 Chaperones | ||||||
![]() | Alkaline phosphatase,Chaperone DnaJ domain-containing protein fusion | ||||||
![]() | CHAPERONE / Client Recognition | ||||||
Function / homology | ![]() oxidoreductase activity, acting on phosphorus or arsenic in donors / alkaline phosphatase / alkaline phosphatase activity / hydrogenase (acceptor) activity / phosphoprotein phosphatase activity / dephosphorylation / protein dephosphorylation / unfolded protein binding / protein folding / outer membrane-bounded periplasmic space ...oxidoreductase activity, acting on phosphorus or arsenic in donors / alkaline phosphatase / alkaline phosphatase activity / hydrogenase (acceptor) activity / phosphoprotein phosphatase activity / dephosphorylation / protein dephosphorylation / unfolded protein binding / protein folding / outer membrane-bounded periplasmic space / periplasmic space / magnesium ion binding / zinc ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
![]() | Jiang, Y. / Rossi, P. / Kalodimos, C.G. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis for client recognition and activity of Hsp40 chaperones. Authors: Jiang, Y. / Rossi, P. / Kalodimos, C.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 594 KB | Display | ![]() |
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PDB format | ![]() | 505.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 406 KB | Display | ![]() |
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Full document | ![]() | 486.3 KB | Display | |
Data in XML | ![]() | 26.9 KB | Display | |
Data in CIF | ![]() | 46.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6pptC ![]() 6pqeC ![]() 6pqmC ![]() 6priC ![]() 6prjC ![]() 6prpC ![]() 6prqC ![]() 6psiC C: citing same article ( |
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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: 9256.687 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Type: solution Contents: 1 mM [U-100% 13C; U-100% 15N] L11-K20_CBD1, 20 mM potassium phosphate, 75 mM potassium chloride, 0.04 % sodium azide, 90% H2O/10% D2O Details: double labeled / Label: 13C-15N_sample / Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 100 mM / Label: conditions_1 / pH: 7.0 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE NEO / Manufacturer: Bruker / Model: AVANCE NEO / Field strength: 700 MHz |
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Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 / Details: restrained molecular dynamics | ||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |