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- PDB-1jw2: SOLUTION STRUCTURE OF HEMOLYSIN EXPRESSION MODULATING PROTEIN Hha... -
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Open data
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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 | ||||||
![]() | HEMOLYSIN EXPRESSION MODULATING PROTEIN Hha | ||||||
![]() | GENE REGULATION / Hha / HEMOLYSIN EXPRESSION MODULATING PROTEIN / Structural Genomics / Protein Structure Initiative / OCSP / NESG / PSI / Northeast Structural Genomics Consortium | ||||||
Function / homology | ![]() H-NS-Hha complex / regulation of gene expression / transcription regulator complex / regulation of DNA-templated transcription / DNA binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / distance geometry simulated annealing | ||||||
![]() | Chang, X. / Yee, A. / Savchenko, A. / Edwards, A.M. / Arrowsmith, C.H. / Northeast Structural Genomics Consortium (NESG) | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 243.6 KB | Display | ![]() |
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PDB format | ![]() | 201 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 341.8 KB | Display | ![]() |
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Full document | ![]() | 417.9 KB | Display | |
Data in XML | ![]() | 16.1 KB | Display | |
Data in CIF | ![]() | 24.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1jcuC ![]() 1jdqC ![]() 1je3C ![]() 1jrmC ![]() 1jw3C ![]() 1ryjC ![]() 1rykC C: citing same article ( |
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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: 8642.016 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 | 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 |