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- PDB-1rzw: The Solution Structure of the Archaeglobus fulgidis protein AF209... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1rzw | ||||||
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Title | The Solution Structure of the Archaeglobus fulgidis protein AF2095. Northeast Structural Genomics Consortium target GR4 | ||||||
![]() | Protein AF2095(GR4) | ||||||
![]() | Structural Genomics / Unknown function / Beta-sheet of 4 parallel / anti-parallel beta-strands and 3 alpha-helices / PSI / Protein Structure Initiative / Northeast Structural Genomics Consortium / NESG | ||||||
Function / homology | ![]() positive regulation of anoikis / peptidyl-tRNA hydrolase / aminoacyl-tRNA hydrolase activity / negative regulation of anoikis / translation / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / distance geometry simulated annealing, molecular dynamics | ||||||
![]() | Powers, R. / Acton, T.B. / Huang, Y.J. / Liu, J. / Ma, L. / Rost, B. / Chiang, Y. / Cort, J.R. / Kennedy, M.A. / Montelione, G.T. / Northeast Structural Genomics Consortium (NESG) | ||||||
![]() | ![]() Title: Solution structure of Archaeglobus fulgidis peptidyl-tRNA hydrolase (Pth2) provides evidence for an extensive conserved family of Pth2 enzymes in archea, bacteria, and eukaryotes Authors: Powers, R. / Mirkovic, N. / Goldsmith-Fischman, S. / Acton, T.B. / Chiang, Y. / Huang, Y.J. / Ma, L. / Rajan, P.K. / Cort, J.R. / Kennedy, M.A. / Liu, J. / Rost, B. / Honig, B. / Murray, D. / Montelione, G.T. #1: Journal: J.Biomol.Nmr / Year: 2004 Title: 1H, 13C and 15N assignments for the Archaeglobus fulgidis protein AF2095. Authors: Powers, R. / Acton, T.B. / Chiang, Y. / Paranji, R. / Cort, J.R. / Kennedy, M.A. / Liu, J. / Ma, L. / Rost, B. / Montelione, G.T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 53.9 KB | Display | ![]() |
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PDB format | ![]() | 40 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 245 KB | Display | ![]() |
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Full document | ![]() | 244.8 KB | Display | |
Data in XML | ![]() | 4.1 KB | Display | |
Data in CIF | ![]() | 5.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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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: 13578.943 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: 20 mM MES, 100 mM NaCl, 5 mM CaCl2, 10 mM DTT, 0.02% NaN3, 5% D2O pH 6.5 Solvent system: 95% H2O/5% D2O |
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Sample conditions | Ionic strength: 20 mM MES, 100 mM NaCl, 5 mM CaCl2, 10 mM DTT, 0.02% NaN3 pH: 6.5 / Pressure: ambient / Temperature: 313 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, molecular dynamics Software ordinal: 1 | ||||||||||||||||||||||||
NMR ensemble | Conformers submitted total number: 1 |