[English] 日本語
![](img/lk-miru.gif)
- PDB-1a03: THE THREE-DIMENSIONAL STRUCTURE OF CA2+-BOUND CALCYCLIN: IMPLICAT... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1a03 | ||||||
---|---|---|---|---|---|---|---|
Title | THE THREE-DIMENSIONAL STRUCTURE OF CA2+-BOUND CALCYCLIN: IMPLICATIONS FOR CA2+-SIGNAL TRANSDUCTION BY S100 PROTEINS, NMR, 20 STRUCTURES | ||||||
![]() | CALCYCLIN (RABBIT, CA2+) | ||||||
![]() | CALCIUM-BINDING PROTEIN / EF-HAND / S-100 PROTEIN | ||||||
Function / homology | ![]() S100 protein binding / cytoplasmic side of plasma membrane / calcium-dependent protein binding / nuclear envelope / collagen-containing extracellular matrix / calcium ion binding / perinuclear region of cytoplasm / extracellular space / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / METRIC MATRIX DISTANCE GEOMETRY, RESTRAINED MOLECULAR DYNAMICS SIMULATED ANNEALING | ||||||
![]() | Sastry, M. / Ketchem, R.R. / Crescenzi, O. / Weber, C. / Lubienski, M.J. / Hidaka, H. / Chazin, W.J. | ||||||
![]() | ![]() Title: The three-dimensional structure of Ca(2+)-bound calcyclin: implications for Ca(2+)-signal transduction by S100 proteins. Authors: Sastry, M. / Ketchem, R.R. / Crescenzi, O. / Weber, C. / Lubienski, M.J. / Hidaka, H. / Chazin, W.J. #1: ![]() Title: 1H NMR Assignments of Apo Calcyclin and Comparative Structural Analysis with Calbindin D9K and S100 Beta Authors: Potts, B.C. / Carlstrom, G. / Okazaki, K. / Hidaka, H. / Chazin, W.J. #2: ![]() Title: The Structure of Calcyclin Reveals a Novel Homodimeric Fold for S100 Ca(2+)-Binding Proteins Authors: Potts, B.C. / Smith, J. / Akke, M. / Macke, T.J. / Okazaki, K. / Hidaka, H. / Case, D.A. / Chazin, W.J. #3: ![]() Title: Erratum. The Structure of Calcyclin Reveals a Novel Homodimeric Fold for S100 Ca(2+)-Binding Proteins Authors: Potts, B.C. / Smith, J. / Akke, M. / Macke, T.J. / Okazaki, K. / Hidaka, H. / Case, D.A. / Chazin, W.J. #4: ![]() Title: A Calcium-Binding Protein from Rabbit Lung Cytosol Identified as the Product of Growth-Regulated Gene (2A9) and its Binding Proteins Authors: Tokumitsu, H. / Kobayashi, R. / Hidaka, H. #5: ![]() Title: Erratum. A Calcium-Binding Protein from Rabbit Lung Cytosol Identified as the Product of Growth-Regulated Gene (2A9) and its Binding Proteins Authors: Tokumitsu, H. / Kobayashi, R. / Hidaka, H. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 1.1 MB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 932.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 366.7 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 575.2 KB | Display | |
Data in XML | ![]() | 56.3 KB | Display | |
Data in CIF | ![]() | 82.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein | Mass: 10167.729 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: RABBIT, CA2+ / Source: (gene. exp.) ![]() ![]() ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
---|---|
NMR experiment | Type: SEE MANUSCRIPT |
-
Sample preparation
Details | Contents: 95% H2O, 5% D2O |
---|---|
Sample conditions | Ionic strength: 50mM TRIS, 20-38mM CACL2 / pH: 7.0 / Temperature: 300 K |
Crystal grow | *PLUS Method: other |
-NMR measurement
NMR spectrometer |
|
---|
-
Processing
NMR software |
| ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: METRIC MATRIX DISTANCE GEOMETRY, RESTRAINED MOLECULAR DYNAMICS SIMULATED ANNEALING Software ordinal: 1 | ||||||||||||||||
NMR ensemble | Conformer selection criteria: LEAST RESTRAINT VIOLATION ENERGY Conformers calculated total number: 192 / Conformers submitted total number: 20 |