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- PDB-1a2x: COMPLEX OF TROPONIN C WITH A 47 RESIDUE (1-47) FRAGMENT OF TROPONIN I -
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Open data
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Basic information
Entry | Database: PDB / ID: 1a2x | ||||||
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Title | COMPLEX OF TROPONIN C WITH A 47 RESIDUE (1-47) FRAGMENT OF TROPONIN I | ||||||
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![]() | COMPLEX (SKELETAL MUSCLE/MUSCLE PROTEIN) / TROPONIN / MUSCLE CONTRACTION REGULATION / COMPLEX (SKELETAL MUSCLE-MUSCLE PROTEIN) / COMPLEX (SKELETAL MUSCLE-MUSCLE PROTEIN) complex | ||||||
Function / homology | ![]() troponin T binding / troponin complex / myosin II complex / skeletal muscle contraction / cardiac muscle contraction / actin binding / calcium ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Vassylyev, D.G. / Takeda, S. / Wakatsuki, S. / Maeda, K. / Maeda, Y. | ||||||
![]() | ![]() Title: Crystal structure of troponin C in complex with troponin I fragment at 2.3-A resolution. Authors: Vassylyev, D.G. / Takeda, S. / Wakatsuki, S. / Maeda, K. / Maeda, Y. #1: ![]() Title: Production, Crystallization, and Preliminary X-Ray Analysis of Rabbit Skeletal Muscle Troponin Complex Consisting of Troponin C and Fragment (1-47) of Troponin I Authors: Saijo, Y. / Takeda, S. / Scherer, A. / Kobayashi, T. / Maeda, Y. / Taniguchi, H. / Yao, M. / Wakatsuki, S. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 52.9 KB | Display | ![]() |
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PDB format | ![]() | 37.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 438.7 KB | Display | ![]() |
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Full document | ![]() | 449.2 KB | Display | |
Data in XML | ![]() | 11.6 KB | Display | |
Data in CIF | ![]() | 15.2 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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Components
#1: Protein | Mass: 17981.785 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||
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#2: Protein/peptide | Mass: 5546.197 Da / Num. of mol.: 1 / Fragment: RESIDUES 1 - 47 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||
#3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 35 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop / pH: 8 Details: HANGING-DROP VAPOR DIFFUSION METHOD WAS USED AT 289K BY MIXING THE PROTEIN SOLUTION CONTAINING 25-30MG/ML OF THE CI47 COMPLEX WITH A RESERVOIR SOLUTION CONTAINING 1.5M SODIUM CITRATE, 0.1M ...Details: HANGING-DROP VAPOR DIFFUSION METHOD WAS USED AT 289K BY MIXING THE PROTEIN SOLUTION CONTAINING 25-30MG/ML OF THE CI47 COMPLEX WITH A RESERVOIR SOLUTION CONTAINING 1.5M SODIUM CITRATE, 0.1M TRIS-HCL, PH 8.0, 15% TREHALOSE., vapor diffusion - hanging drop | ||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 16 ℃ / Method: vapor diffusion, hanging drop / Details: Saijo, Y., (1997) Protein Sci., 6, 916. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Jun 1, 1997 |
Radiation | Monochromator: MONOCHROMATOR / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→25 Å / Num. obs: 8870 / % possible obs: 96.3 % / Observed criterion σ(I): 0 / Redundancy: 4.5 % / Biso Wilson estimate: 45 Å2 / Rmerge(I) obs: 0.05 / Rsym value: 0.05 / Net I/σ(I): 9.2 |
Reflection shell | Resolution: 2.3→2.4 Å / Redundancy: 4.3 % / Rmerge(I) obs: 0.3 / Mean I/σ(I) obs: 2.3 / % possible all: 94 |
Reflection | *PLUS Num. measured all: 37214 |
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Processing
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Refinement | Method to determine structure: SIR/MAD / Resolution: 2.3→10 Å / Data cutoff high absF: 100000000000 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / σ(F): 0
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Displacement parameters | Biso mean: 41 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.3 Å / Luzzati d res low obs: 6 Å / Luzzati sigma a obs: 0.28 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→10 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.3→2.4 Å / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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