[English] 日本語
![](img/lk-miru.gif)
- PDB-2n08: NMR structure of a short hydrophobic 11mer peptide in 25 mM SDS s... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 2n08 | ||||||
---|---|---|---|---|---|---|---|
Title | NMR structure of a short hydrophobic 11mer peptide in 25 mM SDS solution | ||||||
![]() | Short hydrophobic peptide with cyclic constraints | ||||||
![]() | DE NOVO PROTEIN / hydrophobic peptide / GLP-1R agonist | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Hoang, H.N. / Song, K. / Hill, T.A. / Derksen, D.R. / Edmonds, D.J. / Kok, W.M. / Limberakis, C. / Liras, S. / Loria, P.M. / Mascitti, V. ...Hoang, H.N. / Song, K. / Hill, T.A. / Derksen, D.R. / Edmonds, D.J. / Kok, W.M. / Limberakis, C. / Liras, S. / Loria, P.M. / Mascitti, V. / Mathiowetz, A.M. / Mitchell, J.M. / Piotrowski, D.W. / Price, D.A. / Stanton, R.V. / Suen, J.Y. / Withka, J.M. / Griffith, D.A. / Fairlie, D.P. | ||||||
![]() | ![]() Title: Short Hydrophobic Peptides with Cyclic Constraints Are Potent Glucagon-like Peptide-1 Receptor (GLP-1R) Agonists. Authors: Hoang, H.N. / Song, K. / Hill, T.A. / Derksen, D.R. / Edmonds, D.J. / Kok, W.M. / Limberakis, C. / Liras, S. / Loria, P.M. / Mascitti, V. / Mathiowetz, A.M. / Mitchell, J.M. / Piotrowski, D. ...Authors: Hoang, H.N. / Song, K. / Hill, T.A. / Derksen, D.R. / Edmonds, D.J. / Kok, W.M. / Limberakis, C. / Liras, S. / Loria, P.M. / Mascitti, V. / Mathiowetz, A.M. / Mitchell, J.M. / Piotrowski, D.W. / Price, D.A. / Stanton, R.V. / Suen, J.Y. / Withka, J.M. / Griffith, D.A. / Fairlie, D.P. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 60.2 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 44.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 354.1 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 390 KB | Display | |
Data in XML | ![]() | 5.4 KB | Display | |
Data in CIF | ![]() | 7.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2n09C ![]() 2n0iC ![]() 2n0nC C: citing same article ( |
---|---|
Similar structure data | |
Other databases |
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein/peptide | Mass: 1257.308 Da / Num. of mol.: 1 / Source method: obtained synthetically |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
---|---|
NMR experiment | Type: NOESY |
-
Sample preparation
Details | Contents: 1 mM peptide, 25 mM SDS, 100% H2O / Solvent system: 100% H2O | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Sample |
| |||||||||
Sample conditions | Ionic strength: 0.01 / pH: 7.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: Avance / Field strength: 600 MHz |
---|
-
Processing
NMR software |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 1 | |||||||||
NMR constraints | NOE constraints total: 96 / NOE intraresidue total count: 30 / NOE medium range total count: 60 | |||||||||
NMR representative | Selection criteria: lowest energy | |||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 20 / Maximum lower distance constraint violation: 0.2 Å / Maximum upper distance constraint violation: 0.2 Å |