[English] 日本語
![](img/lk-miru.gif)
- PDB-2oru: Solution structure of xtz1-peptide, a beta-hairpin peptide with a... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 2oru | ||||||
---|---|---|---|---|---|---|---|
Title | Solution structure of xtz1-peptide, a beta-hairpin peptide with a structured extension | ||||||
![]() | xtz1-peptide | ||||||
![]() | DE NOVO PROTEIN / hairpin | ||||||
Method | SOLUTION NMR / Simulated annealing, TORSION ANGLE DYNAMICS | ||||||
![]() | Campbell, R.E. | ||||||
![]() | ![]() Title: In Vivo Screening Identifies a Highly Folded beta-Hairpin Peptide with a Structured Extension. Authors: Cheng, Z. / Miskolzie, M. / Campbell, R.E. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 117.2 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 84.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 336.9 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 412.8 KB | Display | |
Data in XML | ![]() | 6.4 KB | Display | |
Data in CIF | ![]() | 9.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein/peptide | Mass: 2551.854 Da / Num. of mol.: 1 / Source method: obtained synthetically |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-
Sample preparation
Details | Contents: 2 mM xtz1-peptide; 90% H2O, 10% D2O, pH 6, 0.010 ml of 0.1% DSS Solvent system: 90% H2O/10% D2O |
---|---|
Sample conditions | Ionic strength: 2 mM peptide / pH: 6 / Pressure: AMBIENT / Temperature: 288 K |
-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, TORSION ANGLE DYNAMICS / Software ordinal: 1 Details: Chemical shift assignments were manually done. Automated NOESY assignment and structure ensemble calculation was performed with CYANA v.2.1. A total of 431 unassigned NOESY peaks with ...Details: Chemical shift assignments were manually done. Automated NOESY assignment and structure ensemble calculation was performed with CYANA v.2.1. A total of 431 unassigned NOESY peaks with intensity greater than ~1% of the most intense NOESY peak were input to CYANA. CYANA assigned 403 of 431 (93.5%) peaks, of which 309 were used as distance constraints in the structure calculation. | ||||||||||||||||||||
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 |