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- PDB-4tnc: REFINED STRUCTURE OF CHICKEN SKELETAL MUSCLE TROPONIN C IN THE TW... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4tnc | |||||||||
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Title | REFINED STRUCTURE OF CHICKEN SKELETAL MUSCLE TROPONIN C IN THE TWO-CALCIUM STATE AT 2-ANGSTROMS RESOLUTION | |||||||||
![]() | TROPONIN C | |||||||||
![]() | CONTRACTILE SYSTEM PROTEIN | |||||||||
Function / homology | ![]() troponin complex / Striated Muscle Contraction / myosin II complex / skeletal muscle contraction / calcium ion binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Sundaralingam, M. | |||||||||
![]() | ![]() Title: Refined structure of chicken skeletal muscle troponin C in the two-calcium state at 2-A resolution. Authors: Satyshur, K.A. / Rao, S.T. / Pyzalska, D. / Drendel, W. / Greaser, M. / Sundaralingam, M. #1: ![]() Title: Molecular Structure of Troponin C from Chicken Skeletal Muscle at 3-Angstrom Resolution Authors: Sundaralingam, M. / Bergstrom, R. / Strasburg, G. / Rao, S.T. / Roychowdhury, P. / Greaser, M. / Wang, B.C. #2: ![]() Title: X-Ray Diffraction Studies of Troponin-C Crystals from Rabbit and Chicken Skeletal Muscles Authors: Strasburg, G.M. / Greaser, M.L. / Sundaralingam, M. #3: ![]() Title: The Amino Acid Sequence of Troponin C from Chicken Skeletal Muscle Authors: Wilkinson, J.M. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 48.2 KB | Display | ![]() |
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PDB format | ![]() | 32.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 372.6 KB | Display | ![]() |
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Full document | ![]() | 406.1 KB | Display | |
Data in XML | ![]() | 9 KB | Display | |
Data in CIF | ![]() | 12 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Atom site foot note | 1: SEE REMARK 4. |
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Components
#1: Protein | Mass: 18262.172 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.14 Å3/Da / Density % sol: 42.46 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 5.1 / Method: other | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2 Å / Lowest resolution: 10 Å / Num. obs: 8861 |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||
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Refinement | Resolution: 2→8 Å /
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Refine analyze | Luzzati coordinate error obs: 0.17 Å | ||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→8 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2 Å / Num. reflection obs: 8100 / Rfactor obs: 0.172 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS |