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- PDB-1bq0: J-DOMAIN (RESIDUES 1-77) OF THE ESCHERICHIA COLI N-TERMINAL FRAGM... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1bq0 | ||||||
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Title | J-DOMAIN (RESIDUES 1-77) OF THE ESCHERICHIA COLI N-TERMINAL FRAGMENT (RESIDUES 1-104) OF THE MOLECULAR CHAPERONE DNAJ, NMR, 20 STRUCTURES | ||||||
![]() | DNAJ | ||||||
![]() | CHAPERONE / HEAT SHOCK / PROTEIN FOLDING / DNAK | ||||||
Function / homology | ![]() sigma factor antagonist activity / protein disulfide isomerase activity / chaperone cofactor-dependent protein refolding / protein-disulfide reductase activity / protein unfolding / heat shock protein binding / viral process / unfolded protein binding / protein folding / protein-folding chaperone binding ...sigma factor antagonist activity / protein disulfide isomerase activity / chaperone cofactor-dependent protein refolding / protein-disulfide reductase activity / protein unfolding / heat shock protein binding / viral process / unfolded protein binding / protein folding / protein-folding chaperone binding / response to heat / protein refolding / protein-containing complex assembly / DNA replication / protein homodimerization activity / protein-containing complex / zinc ion binding / ATP binding / membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / DG, SIMULATED ANNEALING | ||||||
![]() | Huang, K. / Flanagan, J.M. / Prestegard, J.H. | ||||||
![]() | ![]() Title: The influence of C-terminal extension on the structure of the "J-domain" in E. coli DnaJ. Authors: Huang, K. / Flanagan, J.M. / Prestegard, J.H. #1: ![]() Title: 1H and 15N Magnetic Resonance Assignments, Secondary Structure, and Tertiary Fold of Escherichia Coli Dnaj(1-78) Authors: Hill, R.B. / Flanagan, J.M. / Prestegard, J.H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 488.9 KB | Display | ![]() |
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PDB format | ![]() | 406.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 345.5 KB | Display | ![]() |
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Full document | ![]() | 559.1 KB | Display | |
Data in XML | ![]() | 57.6 KB | Display | |
Data in CIF | ![]() | 80 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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: 11417.551 Da / Num. of mol.: 1 / Fragment: N-TERMINAL FRAGMENT (RESIDUES 1-104) 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 | Type: SEE PAPER *JRNL* |
NMR details | Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N LABELED PROTEIN |
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Sample preparation
Details | Contents: 2MM, 10% D2O IN H2O |
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Sample conditions | Ionic strength: 50 mM PHOSPHATE / pH: 6.0 / Temperature: 303 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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Processing
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NMR software |
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Refinement | Method: DG, SIMULATED ANNEALING / Software ordinal: 1 Details: REFINEMENT DETAILS ARE IN THE PRIMARY JOURNAL REFERENCE | |||||||||
NMR ensemble | Conformer selection criteria: ZERO VIOLATIONS/ENERGY (SEE PAPER *JRNL*) Conformers calculated total number: 50 / Conformers submitted total number: 20 |