[English] 日本語
![](img/lk-miru.gif)
- PDB-1zrr: Residual Dipolar Coupling Refinement of Acireductone Dioxygenase ... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1zrr | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Residual Dipolar Coupling Refinement of Acireductone Dioxygenase from Klebsiella | |||||||||
![]() | E-2/E-2' protein | |||||||||
![]() | OXIDOREDUCTASE / nickel / cupin / beta helix / methionine salvage | |||||||||
Function / homology | ![]() acireductone dioxygenase (Ni2+-requiring) / acireductone dioxygenase [iron(II)-requiring] / acireductone dioxygenase (Ni2+-requiring) activity / acireductone dioxygenase [iron(II)-requiring] activity / L-methionine salvage from S-adenosylmethionine / L-methionine salvage from methylthioadenosine / nickel cation binding / iron ion binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | SOLUTION NMR / combined torsional, cartesian dynamics simulated annealing with residual dipolar couplings, NOE, chemical shift, dihedral restraints | |||||||||
![]() | Pochapsky, T.C. / Pochapsky, S.S. / Ju, T. / Hoefler, C. / Liang, J. | |||||||||
![]() | ![]() Title: A refined model for the structure of acireductone dioxygenase from Klebsiella ATCC 8724 incorporating residual dipolar couplings Authors: Pochapsky, T.C. / Pochapsky, S.S. / Ju, T. / Hoefler, C. / Liang, J. #1: Journal: Nat.Struct.Biol. / Year: 2002 Title: Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae Authors: Pochapsky, T.C. / Pochapsky, S.S. / Ju, T. / Mo, H. / Al-Mjeni, F. / Maroney, M.J. #2: Journal: Biochemistry / Year: 2001 Title: Mechanistic Studies of two Dioxygenases from the methionine salvage pathway of Klebsiella pneumoniae Authors: Dai, Y. / Pochapsky, T.C. / Abeles, R.H. | |||||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 921.2 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 784.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 343.9 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 545.4 KB | Display | |
Data in XML | ![]() | 84 KB | Display | |
Data in CIF | ![]() | 110.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein | Mass: 20219.412 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|---|
#2: Chemical | ChemComp-NI / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
---|
-
Sample preparation
Details | Contents: 1 mM aRD 15N labeled in 5% orienting medium (either filamentous phage or C12E5 polymer) pH 7.4, 20 mM KPi; 90/10 H2O/D2O Solvent system: 90/10 H2O/D2O |
---|
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
---|---|
Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
-
Processing
NMR software | Name: ![]() |
---|---|
Refinement | Method: combined torsional, cartesian dynamics simulated annealing with residual dipolar couplings, NOE, chemical shift, dihedral restraints Software ordinal: 1 Details: Metal binding site modeled from XAFS data, paramagnetically broadened backbone residues modeled from pdb entry 1VR3 (ARD homologue from Mus musculus). |
NMR representative | Selection criteria: closest to the average |
NMR ensemble | Conformers submitted total number: 17 |