+Open data
-Basic information
Entry | Database: PDB / ID: 1lg4 | ||||||
---|---|---|---|---|---|---|---|
Title | NMR structure of the human doppel protein fragment 24-152 | ||||||
Components | Prion-like protein | ||||||
Keywords | Prion Protein / prion / doppel / scrapie | ||||||
Function / homology | Function and homology information : / acrosome reaction / Post-translational modification: synthesis of GPI-anchored proteins / intracellular copper ion homeostasis / protein homooligomerization / copper ion binding / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Luhrs, T. / Riek, R. / Guntert, P. / Wuthrich, K. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2003 Title: NMR Structure of the Human Doppel Protein Authors: Luhrs, T. / Riek, R. / Guntert, P. / Wuthrich, K. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1lg4.cif.gz | 606.7 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1lg4.ent.gz | 520.6 KB | Display | PDB format |
PDBx/mmJSON format | 1lg4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1lg4_validation.pdf.gz | 358.4 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1lg4_full_validation.pdf.gz | 497.5 KB | Display | |
Data in XML | 1lg4_validation.xml.gz | 28.8 KB | Display | |
Data in CIF | 1lg4_validation.cif.gz | 51.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lg/1lg4 ftp://data.pdbj.org/pub/pdb/validation_reports/lg/1lg4 | HTTPS FTP |
-Related structure data
Related structure data | |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 14843.668 Da / Num. of mol.: 1 / Fragment: hDpl(24-152) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: Prnd / Plasmid: pRSETA / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21/DE3 / References: UniProt: Q9UKY0 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample conditions | Ionic strength: 10 mM / pH: 4.5 / Pressure: ambient / Temperature: 293 K | ||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
---|---|
Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 750 MHz |
-Processing
NMR software |
| ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR representative | Selection criteria: closest to the average | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 |