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- PDB-1la0: Solution Structure of Calcium Saturated Cardiac Troponin C in the... -

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Basic information

Entry
Database: PDB / ID: 1la0
TitleSolution Structure of Calcium Saturated Cardiac Troponin C in the Troponin C-Troponin I Complex
ComponentsTroponin C, slow skeletal and cardiac muscles
KeywordsCONTRACTILE PROTEIN / EF-hand / troponin
Function / homology
Function and homology information


cardiac Troponin complex / Striated Muscle Contraction / myosin II complex / troponin I binding / skeletal muscle contraction / cardiac muscle contraction / calcium-dependent protein binding / calcium ion binding
Similarity search - Function
EF-hand domain pair / EF-hand / Recoverin; domain 1 / 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 ...EF-hand domain pair / EF-hand / Recoverin; domain 1 / 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 / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Troponin C, slow skeletal and cardiac muscles
Similarity search - Component
Biological speciesGallus gallus (chicken)
MethodSOLUTION NMR / Rigid body minimization
Model type detailsminimized average
AuthorsDvoretsky, A. / Abusamhadneh, E.M. / Howarth, J.W. / Rosevear, P.R.
CitationJournal: J.Biol.Chem. / Year: 2002
Title: Solution Structure of Calcium-Saturated Cardiac Troponin C bound to cardiac Troponin I.
Authors: Dvoretsky, A. / Abusamhadneh, E.M. / Howarth, J.W. / Rosevear, P.R.
History
DepositionMar 27, 2002Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 11, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 28, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_conn_angle / pdbx_struct_oper_list / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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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
hetero molecules


Theoretical massNumber of molelcules
Total (without water)18,5684
Polymers18,4481
Non-polymers1203
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / -
Representativeminimized average structure

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Components

#1: Protein Troponin C, slow skeletal and cardiac muscles / / TN-C


Mass: 18447.535 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / Plasmid: pET23d+ / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P09860
#2: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Ca

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111a/b TROSY
122a/b TROSY
233a/b TROSY

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Sample preparation

Details
Solution-IDContentsSolvent system
1[15N, 2H]cTnC/cTnI complexes10% 2H2O, 20 mM Tris-d11 (pH=6.8), 500 mM KCl, 10 mM CaCl2, 5 mM DTT, 5mM ?-mercaptoethanol, 0.1 mM pefabloc and 0.1 mM leupeptin.
2[15N, 2H]cTnC/cTnI complexes(pH=6.8), 500 mM KCl, 10 mM CaCl2, 5 mM DTT, 5mM ?-mercaptoethanol, 0.1 mM pefabloc and 0.1 mM leupeptin. pF1.
3[15N, 2H]cTnC/cTnI complexes(pH=6.8), 500 mM KCl, 10 mM CaCl2, 5 mM DTT, 5mM ?-mercaptoethanol, 0.1 mM pefabloc and 0.1 mM leupeptin. 4.5% molar ratio of 0.96 (C12E5/n-hexanol) lamellar phase
Sample conditions
Conditions-IDIonic strengthpHPressure (kPa)Temperature (K)
1500 mM KCl, 10 mM CaCl2 6.8 ambient 311 K
2500 mM KCl, 10 mM CaCl2 6.8 ambient 313 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 800 MHz

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Processing

NMR softwareName: X-PLOR / Version: 3.84 / Developer: Brunger/Clore / Classification: refinement
RefinementMethod: Rigid body minimization / Software ordinal: 1
NMR representativeSelection criteria: minimized average structure
NMR ensembleConformers submitted total number: 1

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