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Yorodumi- PDB-1jw2: SOLUTION STRUCTURE OF HEMOLYSIN EXPRESSION MODULATING PROTEIN Hha... -
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-Basic information
Entry | Database: PDB / ID: 1jw2 | ||||||
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Title | SOLUTION STRUCTURE OF HEMOLYSIN EXPRESSION MODULATING PROTEIN Hha FROM ESCHERICHIA COLI. Ontario Centre for Structural Proteomics target EC0308_1_72; Northeast Structural Genomics Target ET88 | ||||||
Components | HEMOLYSIN EXPRESSION MODULATING PROTEIN Hha | ||||||
Keywords | GENE REGULATION / Hha / HEMOLYSIN EXPRESSION MODULATING PROTEIN / Structural Genomics / Protein Structure Initiative / OCSP / NESG / PSI / Northeast Structural Genomics Consortium | ||||||
Function / homology | Function and homology information H-NS-Hha complex / regulation of gene expression / transcription regulator complex / regulation of DNA-templated transcription / DNA binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / distance geometry simulated annealing | ||||||
Authors | Chang, X. / Yee, A. / Savchenko, A. / Edwards, A.M. / Arrowsmith, C.H. / Northeast Structural Genomics Consortium (NESG) | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2002 Title: An NMR approach to structural proteomics Authors: Yee, A. / Chang, X. / Pineda-Lucena, A. / Wu, B. / Semesi, A. / Le, B. / Ramelot, T. / Lee, G.M. / Bhattacharyya, S. / Gutierrez, P. / Denisov, A. / Lee, C.H. / Cort, J.R. / Kozlov, G. / ...Authors: Yee, A. / Chang, X. / Pineda-Lucena, A. / Wu, B. / Semesi, A. / Le, B. / Ramelot, T. / Lee, G.M. / Bhattacharyya, S. / Gutierrez, P. / Denisov, A. / Lee, C.H. / Cort, J.R. / Kozlov, G. / Liao, J. / Finak, G. / Chen, L. / Wishart, D. / Lee, W. / McIntosh, L.P. / Gehring, K. / Kennedy, M.A. / Edwards, A.M. / Arrowsmith, C.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jw2.cif.gz | 243.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jw2.ent.gz | 201 KB | Display | PDB format |
PDBx/mmJSON format | 1jw2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1jw2_validation.pdf.gz | 341.8 KB | Display | wwPDB validaton report |
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Full document | 1jw2_full_validation.pdf.gz | 417.9 KB | Display | |
Data in XML | 1jw2_validation.xml.gz | 16.1 KB | Display | |
Data in CIF | 1jw2_validation.cif.gz | 24.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jw/1jw2 ftp://data.pdbj.org/pub/pdb/validation_reports/jw/1jw2 | HTTPS FTP |
-Related structure data
Related structure data | 1jcuC 1jdqC 1je3C 1jrmC 1jw3C 1ryjC 1rykC C: citing same article (ref.) |
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Similar structure data | |
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: 8642.016 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PET15B / Production host: Escherichia coli (E. coli) / References: UniProt: P0ACE3 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 2mM Hha U-15N, 13C; Solvent system: 150 mM NACL, 25 mM PHOSPHATE, 10% D2O, PH 6.5 |
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Sample conditions | Ionic strength: 150 mM NACL / pH: 6.5 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: distance geometry simulated annealing / Software ordinal: 1 Details: the structures are based on a total of 1116 restraints, 968 are NOE-derived distance constraints, 96 dihedral angle restraints,52 distance restraints from hydrogen bonds. | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 30 / Conformers submitted total number: 10 |