[English] 日本語
Yorodumi- PDB-2gmg: Solution NMR Structure of protein PF0610 from Pyrococcus furiosus... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2gmg | ||||||
---|---|---|---|---|---|---|---|
Title | Solution NMR Structure of protein PF0610 from Pyrococcus furiosus, Northeast Structural Genomics Consortium Target PfG3 | ||||||
Components | hypothetical protein Pf0610 | ||||||
Keywords | DNA BINDING PROTEIN / winged-helix like protein with metal binding site / Structural Genomics / PSI / Protein Structure Initiative / Northeast Structural Genomics Consortium / NESG | ||||||
Function / homology | Transcriptional regulator containing an HTH domain fused to a Zn-ribbon, predicted / Winged helix DNA-binding domain superfamily / Uncharacterized protein Function and homology information | ||||||
Biological species | Pyrococcus furiosus (archaea) | ||||||
Method | SOLUTION NMR / simulated annealing using torsion angle dynamics | ||||||
Authors | Wang, X. / Lee, H.S. / Adams, M.W. / Northeast Structural Genomics Consortium (NESG) / Montelione, G.T. / Prestegard, J.H. | ||||||
Citation | Journal: Biochemistry / Year: 2007 Title: PF0610, a novel winged helix-turn-helix variant possessing a rubredoxin-like Zn ribbon motif from the hyperthermophilic archaeon, Pyrococcus furiosus. Authors: Wang, X. / Lee, H.S. / Sugar, F.J. / Jenney, F.E. / Adams, M.W. / Prestegard, J.H. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2gmg.cif.gz | 351.6 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2gmg.ent.gz | 292.7 KB | Display | PDB format |
PDBx/mmJSON format | 2gmg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2gmg_validation.pdf.gz | 360.9 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 2gmg_full_validation.pdf.gz | 431.7 KB | Display | |
Data in XML | 2gmg_validation.xml.gz | 16.6 KB | Display | |
Data in CIF | 2gmg_validation.cif.gz | 29.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gm/2gmg ftp://data.pdbj.org/pub/pdb/validation_reports/gm/2gmg | HTTPS FTP |
-Related structure data
Similar structure data | |
---|---|
Other databases |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 12168.449 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pyrococcus furiosus (archaea) / Strain: DSM 3638 / Gene: AE010183 / Plasmid: pET-24d / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q8U362 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Contents: 0.5mM Pf0610 U-15N, 13C, 20mM Tris, 150mM NaCl, 95% H2O, 5% D2O Solvent system: 95% H2O/5% D2O |
---|---|
Sample conditions | Ionic strength: 0.15M / pH: 8.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
|
-Processing
NMR software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing using torsion angle dynamics / Software ordinal: 1 Details: The structure was refined with 923 NOE-derived distance restraints, 109 back bone dihedral angle restraints and 208 residual dipolar coupling constants | ||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 50 / Conformers submitted total number: 10 |