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- PDB-7swi: cTnC-TnI chimera complexed with A2 -

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Basic information

Entry
Database: PDB / ID: 7swi
TitlecTnC-TnI chimera complexed with A2
ComponentsTroponin C, slow skeletal and cardiac muscles,Troponin I, cardiac muscle chimera
KeywordsMETAL BINDING PROTEIN / cardiac troponin / calcium sensitizer
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
Troponin I residues 1-32 / Troponin I residues 1-32 / Troponin / Troponin domain superfamily / Troponin / EF-hand domain pair / EF-hand domain pair / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. ...Troponin I residues 1-32 / Troponin I residues 1-32 / Troponin / Troponin domain superfamily / Troponin / EF-hand domain pair / EF-hand domain pair / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair
Similarity search - Domain/homology
Chem-C9W / Troponin I, cardiac muscle / Troponin C, slow skeletal and cardiac muscles
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
AuthorsPoppe, L. / Hartman, J.J. / Romero, A. / Reagan, J.D.
Funding support United States, 1items
OrganizationGrant numberCountry
Other private United States
CitationJournal: Biochemistry / Year: 2022
Title: Structural and Thermodynamic Model for the Activation of Cardiac Troponin.
Authors: Poppe, L. / Hartman, J.J. / Romero, A. / Reagan, J.D.
History
DepositionNov 19, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 6, 2022Provider: repository / Type: Initial release
Revision 1.1Apr 13, 2022Group: Database references / Category: citation
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Apr 27, 2022Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.3May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Troponin C, slow skeletal and cardiac muscles,Troponin I, cardiac muscle chimera
hetero molecules


Theoretical massNumber of molelcules
Total (without water)14,6852
Polymers14,2221
Non-polymers4621
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: NMR Distance Restraints
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 100target function
RepresentativeModel #1target function

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Components

#1: Protein Troponin C, slow skeletal and cardiac muscles,Troponin I, cardiac muscle chimera / TN-C / Cardiac troponin I


Mass: 14222.121 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TNNC1, TNNC, TNNI3, TNNC1 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P63316, UniProt: P19429
#2: Chemical ChemComp-C9W / 4-(3-cyano-3-methylazetidine-1-carbonyl)-N-[(3R,4S)-7-fluoro-4-hydroxy-6-methyl-3,4-dihydro-2H-1-benzopyran-3-yl]-5-methyl-1H-pyrrole-2-sulfonamide


Mass: 462.495 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C21H23FN4O5S / Feature type: SUBJECT OF INVESTIGATION
Has ligand of interestY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
111isotropic12D 1H-13C HSQC
121isotropic12D 1H-15N HSQC
131isotropic13D CBCA(CO)NH
141isotropic13D CBCANH
151isotropic13D 1H-13C NOESY aliphatic
161isotropic13D 1H-13C NOESY aromatic
171isotropic13D 1H-15N NOESY
181isotropic1X-filtered NOESY
191isotropic13D HBHA(CO)NH
1101isotropic13D HNCO

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Sample preparation

DetailsType: solution
Contents: 1 mM [U-13C; U-15N] cTnC-TnI chimera, 95% H2O/5% D2O
Label: Sample_1 / Solvent system: 95% H2O/5% D2O
SampleConc.: 1 mM / Component: cTnC-TnI chimera / Isotopic labeling: [U-13C; U-15N]
Sample conditionsIonic strength: 50 mM / Label: sample_1 / pH: 7.2 / Pressure: 1 atm / Temperature: 293 K

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NMR measurement

NMR spectrometerType: Bruker AVANCE III HD / Manufacturer: Bruker / Model: AVANCE III HD / Field strength: 800 MHz

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Processing

NMR software
NameVersionDeveloperClassification
TopSpin3Bruker Biospinprocessing
AutoAssign2.3.0Zimmerman, Moseley, Kulikowski and Montelionechemical shift assignment
XEASY1.5.5Bartels et al.peak picking
CYANA3.98.13Guntert, Mumenthaler and Wuthrichrefinement
CYANA3.98.13Guntert, Mumenthaler and Wuthrichstructure calculation
RefinementMethod: simulated annealing / Software ordinal: 4
NMR representativeSelection criteria: target function
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 10

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