[English] 日本語
Yorodumi- PDB-1p68: Solution structure of S-824, a de novo designed four helix bundle -
+Open data
-Basic information
Entry | Database: PDB / ID: 1p68 | ||||||
---|---|---|---|---|---|---|---|
Title | Solution structure of S-824, a de novo designed four helix bundle | ||||||
Components | De novo designed protein S-824 | ||||||
Keywords | DE NOVO PROTEIN / Protein / four helix bundle / de novo design | ||||||
Function / homology | Designed four-helix bundle protein / hypothetical protein mp506/mpn330, domain 1 / Up-down Bundle / Mainly Alpha Function and homology information | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Wei, Y. / Kim, S. / Fela, D. / Baum, J. / Hecht, M.H. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.Usa / Year: 2003 Title: Solution structure of a de novo protein from a designed combinatorial library. Authors: Wei, Y. / Kim, S. / Fela, D. / Baum, J. / Hecht, M.H. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1p68.cif.gz | 481.5 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1p68.ent.gz | 401.8 KB | Display | PDB format |
PDBx/mmJSON format | 1p68.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1p68_validation.pdf.gz | 341.3 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1p68_full_validation.pdf.gz | 481.1 KB | Display | |
Data in XML | 1p68_validation.xml.gz | 50.9 KB | Display | |
Data in CIF | 1p68_validation.cif.gz | 66.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p6/1p68 ftp://data.pdbj.org/pub/pdb/validation_reports/p6/1p68 | HTTPS FTP |
-Related structure data
Similar structure data | |
---|---|
Other databases |
|
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 11949.376 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: pET3a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||||||
NMR details | Text: This structure was determined using standard 3D heteronuclear techniques. |
-Sample preparation
Details | Contents: 50mM Acetate buffer / Solvent system: 92% H2O, 8% D2O |
---|---|
Sample conditions | Ionic strength: 50mM / pH: 4 / Pressure: 1 atm / Temperature: 298 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: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
-Processing
NMR software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||
NMR ensemble | Conformer selection criteria: back calculated data agree with experimental NOESY spectrum Conformers calculated total number: 100 / Conformers submitted total number: 15 |