+Open data
-Basic information
Entry | Database: PDB / ID: 2myj | ||||||
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Title | Solution structure of a bacterial chaperone | ||||||
Components | Acid stress chaperone HdeB | ||||||
Keywords | CHAPERONE | ||||||
Function / homology | Function and homology information cellular stress response to acidic pH / response to acidic pH / unfolded protein binding / outer membrane-bounded periplasmic space Similarity search - Function | ||||||
Biological species | Escherichia coli K-12 (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Jin, C. / Hu, Y. / Ding, J. | ||||||
Citation | Journal: Sci Rep / Year: 2015 Title: HdeB chaperone activity is coupled to its intrinsic dynamic properties. Authors: Ding, J. / Yang, C. / Niu, X. / Hu, Y. / Jin, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2myj.cif.gz | 967.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2myj.ent.gz | 845 KB | Display | PDB format |
PDBx/mmJSON format | 2myj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2myj_validation.pdf.gz | 416.6 KB | Display | wwPDB validaton report |
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Full document | 2myj_full_validation.pdf.gz | 572.6 KB | Display | |
Data in XML | 2myj_validation.xml.gz | 53.3 KB | Display | |
Data in CIF | 2myj_validation.cif.gz | 78.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/my/2myj ftp://data.pdbj.org/pub/pdb/validation_reports/my/2myj | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 9074.217 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli K-12 (bacteria) / Strain: K12 / Gene: hdeB, yhhD, yhiC, b3509, JW5669 / Production host: Escherichia coli (E. coli) / References: UniProt: P0AET2 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 0.17 / pH: 4.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | |||||||||
NMR representative | Selection criteria: lowest energy | |||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |