+Open data
-Basic information
Entry | Database: PDB / ID: 1mxl | ||||||
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Title | STRUCTURE OF CARDIAC TROPONIN C-TROPONIN I COMPLEX | ||||||
Components |
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Keywords | CALCIUM-BINDING PROTEIN / TROPONIN / MUSCLE CONTRACTION / REGULATORY PROTEIN | ||||||
Function / homology | Function and homology information regulation of systemic arterial blood pressure by ischemic conditions / regulation of muscle filament sliding speed / troponin T binding / diaphragm contraction / troponin C binding / regulation of ATP-dependent activity / cardiac Troponin complex / cardiac myofibril / regulation of smooth muscle contraction / troponin complex ...regulation of systemic arterial blood pressure by ischemic conditions / regulation of muscle filament sliding speed / troponin T binding / diaphragm contraction / troponin C binding / regulation of ATP-dependent activity / cardiac Troponin complex / cardiac myofibril / regulation of smooth muscle contraction / troponin complex / regulation of muscle contraction / transition between fast and slow fiber / negative regulation of ATP-dependent activity / Striated Muscle Contraction / regulation of cardiac muscle contraction by calcium ion signaling / response to metal ion / ventricular cardiac muscle tissue morphogenesis / myosin II complex / heart contraction / troponin I binding / skeletal muscle contraction / calcium channel inhibitor activity / vasculogenesis / cardiac muscle contraction / Ion homeostasis / sarcomere / intracellular calcium ion homeostasis / calcium-dependent protein binding / actin filament binding / actin binding / heart development / protein domain specific binding / calcium ion binding / protein kinase binding / protein homodimerization activity / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Li, M.X. / Spyracopoulos, L. / Sykes, B.D. | ||||||
Citation | Journal: Biochemistry / Year: 1999 Title: Binding of cardiac troponin-I147-163 induces a structural opening in human cardiac troponin-C. Authors: Li, M.X. / Spyracopoulos, L. / Sykes, B.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mxl.cif.gz | 1.2 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1mxl.ent.gz | 1 MB | Display | PDB format |
PDBx/mmJSON format | 1mxl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1mxl_validation.pdf.gz | 357.4 KB | Display | wwPDB validaton report |
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Full document | 1mxl_full_validation.pdf.gz | 948.7 KB | Display | |
Data in XML | 1mxl_validation.xml.gz | 102.6 KB | Display | |
Data in CIF | 1mxl_validation.cif.gz | 144.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mx/1mxl ftp://data.pdbj.org/pub/pdb/validation_reports/mx/1mxl | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 10070.304 Da / Num. of mol.: 1 / Fragment: REGULATORY N-DOMAIN RESIDUES 1-89 Source method: isolated from a genetically manipulated source Details: CALCIUM SATURATED N-DOMAIN OF CARDIAC TROPONIN C IN COMPLEX WITH CARDIAC TROPONIN I 147-163 Source: (gene. exp.) Homo sapiens (human) / Strain: BL21(DE3) PLYSS / Tissue: MUSCLE / Description: HOMO SAPIENS / Organ: HEART / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) PLYSS / Tissue (production host): MUSCLE / References: UniProt: P63316 |
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#2: Protein/peptide | Mass: 1806.183 Da / Num. of mol.: 1 / Fragment: CARDIAC TROPONIN I RESIDUES 147-163 / Source method: obtained synthetically Details: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. ITS PARENT PROTEIN IS NATURALLY FOUND IN HEART TISSUE OF HOMO SAPIENS (HUMAN). References: UniProt: P19429 |
#3: Chemical | ChemComp-CA / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED TROPONIN C AND A SYNTHETIC TROPONIN I PEPTIDE |
-Sample preparation
Details | Contents: 10% WATER/90% D2O |
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Sample conditions | pH: 6.7 / Pressure: 1 atm / Temperature: 303 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. | ||||||||||||
NMR ensemble | Conformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 100 / Conformers submitted total number: 40 |