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- PDB-1tnq: STRUCTURES OF THE APO AND CALCIUM TROPONIN-C REGULATORY DOMAINS: ... -
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Basic information
Entry | Database: PDB / ID: 1tnq | ||||||
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Title | STRUCTURES OF THE APO AND CALCIUM TROPONIN-C REGULATORY DOMAINS: THE MUSCLE CONTRACTION SWITCH | ||||||
![]() | TROPONIN-C | ||||||
![]() | CALCIUM-BINDING PROTEIN / EF-HAND | ||||||
Function / homology | ![]() troponin complex / Striated Muscle Contraction / myosin II complex / skeletal muscle contraction / calcium ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Gagne, S.M. / Sykes, B.D. | ||||||
![]() | ![]() Title: Structures of the troponin C regulatory domains in the apo and calcium-saturated states. Authors: Gagne, S.M. / Tsuda, S. / Li, M.X. / Smillie, L.B. / Sykes, B.D. #1: ![]() Title: Quantification of the Calcium-Induced Secondary Structural Changes in the Regulatory Domain of Troponin-C Authors: Gagne, S.M. / Tsuda, S. / Li, M.X. / Chandra, M. / Smillie, L.B. / Sykes, B.D. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1 MB | Display | ![]() |
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PDB format | ![]() | 878.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 353.5 KB | Display | ![]() |
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Full document | ![]() | 672.8 KB | Display | |
Data in XML | ![]() | 61.4 KB | Display | |
Data in CIF | ![]() | 98.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 9984.085 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
NMR software | Name: DGII / Developer: HAVEL / Classification: refinement |
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NMR ensemble | Conformers submitted total number: 40 |