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Yorodumi- PDB-1tnp: STRUCTURES OF THE APO AND CALCIUM TROPONIN-C REGULATORY DOMAINS: ... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 1tnp | ||||||
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| Title | STRUCTURES OF THE APO AND CALCIUM TROPONIN-C REGULATORY DOMAINS: THE MUSCLE CONTRACTION SWITCH | ||||||
Components | TROPONIN-C (APO) | ||||||
Keywords | CALCIUM-BINDING PROTEIN / EF-HAND | ||||||
| Function / homology | Function and homology informationStriated Muscle Contraction / troponin complex / skeletal muscle contraction / calcium ion binding Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | SOLUTION NMR | ||||||
Authors | Gagne, S.M. / Sykes, B.D. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 1995Title: 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: Journal: Protein Sci. / Year: 1994Title: 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: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1tnp.cif.gz | 1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb1tnp.ent.gz | 873.4 KB | Display | PDB format |
| PDBx/mmJSON format | 1tnp.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1tnp_validation.pdf.gz | 340.3 KB | Display | wwPDB validaton report |
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| Full document | 1tnp_full_validation.pdf.gz | 650.1 KB | Display | |
| Data in XML | 1tnp_validation.xml.gz | 55.9 KB | Display | |
| Data in CIF | 1tnp_validation.cif.gz | 88.9 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tn/1tnp ftp://data.pdbj.org/pub/pdb/validation_reports/tn/1tnp | HTTPS FTP |
-Related structure data
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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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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-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 |
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