[English] 日本語
![](img/lk-miru.gif)
- PDB-1prs: NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S COM... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1prs | ||||||
---|---|---|---|---|---|---|---|
Title | NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S COMPLEXED WITH CALCIUM | ||||||
![]() | DEVELOPMENT-SPECIFIC PROTEIN S | ||||||
![]() | BINDING PROTEIN | ||||||
Function / homology | ![]() sporulation resulting in formation of a cellular spore / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Bagby, S. / Harvey, T.S. / Eagle, S.G. / Inouye, S. / Ikura, M. | ||||||
![]() | ![]() Title: NMR-derived three-dimensional solution structure of protein S complexed with calcium. Authors: Bagby, S. / Harvey, T.S. / Eagle, S.G. / Inouye, S. / Ikura, M. #1: ![]() Title: Structural Similarity of a Developmentally Regulated Bacterial Spore Coat Protein to Betagamma-Crystallins of the Vertebrate Eye Lens Authors: Bagby, S. / Harvey, T.S. / Eagle, S.G. / Inouye, S. / Ikura, M. #2: ![]() Title: Unusual Helix-Containing Greek Keys in Development-Specific Ca2+-Binding Protein S. 1H, 15N and 13C Assignments and Secondary Structure Determined Using Multidimensional Double and Triple ...Title: Unusual Helix-Containing Greek Keys in Development-Specific Ca2+-Binding Protein S. 1H, 15N and 13C Assignments and Secondary Structure Determined Using Multidimensional Double and Triple Resonance Heteronuclear NMR Spectroscopy Authors: Bagby, S. / Harvey, T.S. / Kay, L.E. / Eagle, S.G. / Inouye, S. / Ikura, M. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 1.5 MB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 1.2 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 354.3 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 676 KB | Display | |
Data in XML | ![]() | 136 KB | Display | |
Data in CIF | ![]() | 181.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
Atom site foot note | 1: SURFACE LOOPS AT RESIDUES 33 - 40, 72 - 80, 123 - 129, AND 159 - 168 ARE RELATIVELY POORLY DEFINED. | |||||||||
NMR ensembles |
|
-
Components
#1: Protein | Mass: 18805.865 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
---|---|
#2: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
---|
-
Processing
Software |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
NMR software | Name: ![]() | ||||||||
NMR ensemble | Conformers submitted total number: 30 |