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- PDB-1scv: NMR STRUCTURE OF THE C TERMINAL DOMAIN OF CARDIAC TROPONIN C BOUN... -

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Basic information

Entry
Database: PDB / ID: 1scv
TitleNMR STRUCTURE OF THE C TERMINAL DOMAIN OF CARDIAC TROPONIN C BOUND TO THE N TERMINAL DOMAIN OF CARDIAC TROPONIN I
ComponentsTroponin C, slow skeletal and cardiac muscles
KeywordsCONTRACTILE PROTEIN / STRUCTURAL PROTEIN / TROPONIN C-TROPONIN I INTERACTION / CARDIAC / MUSCLE PROTEIN / CALCIUM BINDING PROTEIN
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 / 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 / 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 / DGSA
AuthorsFinley, N.L. / Howarth, J.W. / Rosevear, P.R.
Citation
Journal: Biochemistry / Year: 2004
Title: Structure of the Mg2+-loaded C-lobe of cardiac troponin C bound to the N-domain of cardiac troponin I: comparison with the Ca2+-loaded structure.
Authors: Finley, N.L. / Howarth, J.W. / Rosevear, P.R.
#1: Journal: Biochemistry / Year: 1999
Title: Solution structures of the C-terminal domain of cardiac troponin C free and bound to the N-terminal domain of cardiac troponin I
Authors: Gasmi-Seabrook, G.M. / Howarth, J.W. / Finley, N. / Abusamhadneh, E. / Gaponenko, V. / Brito, R.M. / Solaro, R.J. / Rosevear, P.R.
History
DepositionFeb 12, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 23, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 29, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / 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_nmr_software.name / _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
Remark 650HELIX DETERMINATION METHOD: AUTHOR
Remark 700SHEET DETERMINATION METHOD: AUTHOR

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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)9,5443
Polymers9,4641
Non-polymers802
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 20structures with the lowest energy
RepresentativeModel #7lowest energy

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Components

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


Mass: 9463.531 Da / Num. of mol.: 1 / Fragment: C-terminal domain (RESIDUES 81 - 161)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / Gene: TNNC1 / Plasmid: PET-23D+ / 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.: 2 / 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
11115N-HSQC, 15N-NOESY-HSQC
12115N-TOCSY-HSQC, HNCO, HN(CA)CB
131(HB)CBCA(CO)NNH, H(CCO)NH
141C(CO)NH, (HB)CB(CGCD)HD
151(HB)CB(CGCDCE)HE, CN-NOESY-HSQC, HNHA, HNHB
161AB-TROSY
NMR detailsText: BEST 20 STRUCTURES. THESE STRUCTURES WERE DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON CA2+_SATURATED 15N, 13C-CTNC(81-161) BOUND TO CTNI(33-80).

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Sample preparation

DetailsContents: 1MM [15N,13C]CTNC(81-161)/CTNI(33-80), 20MM TRIS-D11, 100MM KCL, 20MM DTT, 15MM CACL2, 0.1MM LEUPETIN, 0.1MM PEFABLOC; 90% H2O, 10% D2O
Solvent system: 90% H2O/10% D2O
Sample conditionsIonic strength: 100mM KCL, 15mM CACL2 / pH: 6.80 / Pressure: AMBIENT / Temperature: 318.00 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian INOVAVarianINOVA6001
Varian INOVAVarianINOVA8002

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Processing

NMR software
NameVersionDeveloperClassification
Felix2000Accelrysprocessing
CNS1Brungerrefinement
CNX1Accelrysrefinement
RefinementMethod: DGSA / Software ordinal: 1
Details: The structures are based on a total of 926 restraints, 787 are NOE-derived distance restraints, 91 dihedral angle restraints, 4 distance restraints from hydrogen bonds and 44 dipolar coupling restraints.
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 20 / Conformers submitted total number: 20

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