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- PDB-1xbl: NMR STRUCTURE OF THE J-DOMAIN (RESIDUES 2-76) IN THE ESCHERICHIA ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1xbl | ||||||
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Title | NMR STRUCTURE OF THE J-DOMAIN (RESIDUES 2-76) IN THE ESCHERICHIA COLI N-TERMINAL FRAGMENT (RESIDUES 2-108) OF THE MOLECULAR CHAPERONE DNAJ, 20 STRUCTURES | ||||||
![]() | DNAJ | ||||||
![]() | CHAPERONE / DNA REPLICATION / HEAT SHOCK | ||||||
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 / REDAC | ||||||
![]() | Pellecchia, M. / Szyperski, T. / Wall, D. / Georgopoulos, C. / Wuthrich, K. | ||||||
![]() | ![]() Title: NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone. Authors: Pellecchia, M. / Szyperski, T. / Wall, D. / Georgopoulos, C. / Wuthrich, K. #1: ![]() Title: NMR Structure Determination of the Escherichia Coli Dnaj Molecular Chaperone: Secondary Structure and Backbone Fold of the N-Terminal Region (Residues 2-108) Containing the Highly Conserved J Domain Authors: Szyperski, T. / Pellecchia, M. / Wall, D. / Georgopoulos, C. / Wuthrich, K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 545.1 KB | Display | ![]() |
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PDB format | ![]() | 460.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 360.3 KB | Display | ![]() |
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Full document | ![]() | 497.8 KB | Display | |
Data in XML | ![]() | 22.2 KB | Display | |
Data in CIF | ![]() | 38 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar 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: 11846.043 Da / Num. of mol.: 1 Fragment: N-TERMINAL FRAGMENT (RESIDUES 2-108) OF THE MOLECULAR CHAPERONE DNAJ 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* |
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Sample preparation
Sample conditions | pH: 6.0 / Temperature: 301 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: REDAC / Software ordinal: 1 | |||||||||
NMR ensemble | Conformer selection criteria: TARGET FUNCTION (SEE PAPER *JRNL*) Conformers calculated total number: 50 / Conformers submitted total number: 20 |