[English] 日本語
![](img/lk-miru.gif)
- PDB-7d37: Solution structure of Acm2-precursor peptide of Heat-stable enter... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 7d37 | ||||||
---|---|---|---|---|---|---|---|
Title | Solution structure of Acm2-precursor peptide of Heat-stable enterotoxin produced by Enterotoxigenic Escherichia coli | ||||||
![]() | CYS-CY1-GLU-LEU-CYS-CYS-ASN-PRO-ALA-CY1-THR-GLY-CYS | ||||||
![]() | TOXIN / Heat-stable enterotoxin / topological isomer / STh / STh(6-18) | ||||||
Function / homology | Heat-stable enterotoxin, STa / Heat-stable enterotoxin, conserved site / Heat-stable enterotoxin ST / Heat-stable enterotoxins signature. / toxin activity / extracellular space / Heat-stable enterotoxin A3/A4![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Shimamoto, S. / Hidaka, Y. | ||||||
![]() | ![]() Title: Topological Regulation of the Bioactive Conformation of a Disulfide-Rich Peptide, Heat-Stable Enterotoxin. Authors: Shimamoto, S. / Fukutsuji, M. / Osumi, T. / Goto, M. / Toyoda, H. / Hidaka, Y. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 35.1 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 26.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 368.4 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 404.4 KB | Display | |
Data in XML | ![]() | 5.2 KB | Display | |
Data in CIF | ![]() | 6.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7cssC C: citing same article ( |
---|---|
Similar structure data | |
Other databases |
|
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein/peptide | Mass: 1461.751 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() ![]() |
---|---|
Has ligand of interest | Y |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-
Sample preparation
Details |
| ||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample |
| ||||||||||||||||||
Sample conditions | Ionic strength: 1 mM / Label: conditions_1 / pH: 3.0 / Pressure: 1.0 atm / Temperature: 298.15 K |
-NMR measurement
NMR spectrometer | Type: JEOL JNM ECA800 / Manufacturer: JEOL / Model: JNM ECA800 / Field strength: 800 MHz |
---|
-
Processing
NMR software | Name: CNS / Developer: Brunger, Adams, Clore, Gros, Nilges and Read / Classification: structure calculation |
---|---|
Refinement | Method: simulated annealing / Software ordinal: 4 |
NMR representative | Selection criteria: lowest energy |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 1000 / Conformers submitted total number: 10 |