[English] 日本語
![](img/lk-miru.gif)
- PDB-2lvh: Solution structure of the zinc finger AFV1p06 protein from the hy... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 2lvh | ||||||
---|---|---|---|---|---|---|---|
Title | Solution structure of the zinc finger AFV1p06 protein from the hyperthermophilic archaeal virus AFV1 | ||||||
![]() | Putative zinc finger protein ORF59a | ||||||
![]() | METAL BINDING PROTEIN / Zinc finger | ||||||
Function / homology | Classic Zinc Finger / Double Stranded RNA Binding Domain / Zinc finger C2H2 type domain profile. / Zinc finger C2H2 superfamily / Zinc finger C2H2-type / 2-Layer Sandwich / metal ion binding / Alpha Beta / Putative zinc finger protein ORF59a![]() | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing, torsion angle dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
![]() | Guilliere, F. / Sezonov, G. / Prangishvili, D. / Delepierre, M. / Guijarro, J. | ||||||
![]() | ![]() Title: Solution structure of an archaeal DNA binding protein with an eukaryotic zinc finger fold. Authors: Guilliere, F. / Danioux, C. / Jaubert, C. / Desnoues, N. / Delepierre, M. / Prangishvili, D. / Sezonov, G. / Guijarro, J.I. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 157.6 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 126.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Similar structure data | |
---|---|
Other databases |
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein | Mass: 7010.232 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|---|
#2: Chemical | ChemComp-ZN / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-
Sample preparation
Details | Contents: 0.8-1 mM [U-98% 13C; U-98% 15N] AFV1p06, 88% H2O/12% D2O Solvent system: 88% H2O/12% D2O |
---|---|
Sample | Units: mM / Component: AFV1p06-1 / Isotopic labeling: [U-98% 13C; U-98% 15N] / Conc. range: 0.8-1 |
Sample conditions | Ionic strength: 200 / pH: 7.4 / Pressure: ambient / Temperature: 298.15 K |
-NMR measurement
NMR spectrometer | Type: Varian NMR System / Manufacturer: Varian / Model: NMR System / Field strength: 600 MHz |
---|
-
Processing
NMR software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing, torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 959 / NOE intraresidue total count: 380 / NOE long range total count: 220 / NOE medium range total count: 157 / NOE sequential total count: 202 / Hydrogen bond constraints total count: 19 / Protein phi angle constraints total count: 40 / Protein psi angle constraints total count: 37 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 150 / Conformers submitted total number: 10 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NMR ensemble rms | Distance rms dev: 0.0194 Å / Distance rms dev error: 0.0037 Å |