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- PDB-1fi5: NMR STRUCTURE OF THE C TERMINAL DOMAIN OF CARDIAC TROPONIN C BOUN... -

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Basic information

Entry
Database: PDB / ID: 1fi5
TitleNMR STRUCTURE OF THE C TERMINAL DOMAIN OF CARDIAC TROPONIN C BOUND TO THE N TERMINAL DOMAIN OF CARDIAC TROPONIN I.
ComponentsPROTEIN (TROPONIN C)
KeywordsCONTRACTILE 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
AuthorsGasmi-Seabrook, G.M. / Howarth, J.W. / Finley, N. / Abusamhadneh, E. / Gaponenko, V. / Brito, R.M. / Solaro, R.J. / Rosevear, P.R.
CitationJournal: 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
DepositionAug 3, 2000Deposition site: RCSB / Processing site: RCSB
SupersessionAug 23, 2000ID: 1GGS
Revision 1.0Aug 23, 2000Provider: repository / Type: Initial release
Revision 1.1Apr 27, 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: PROTEIN (TROPONIN C)
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 / 500SMALLEST RMSD TO AVERAGE STRUCTURE
RepresentativeModel #5closest to the average

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Components

#1: Protein PROTEIN (TROPONIN C)


Mass: 9463.531 Da / Num. of mol.: 1 / Fragment: RESIDUES 81 - 161
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / Tissue: MUSCLE
Description: C TERMINAL DOMAIN OF CARDIAC TROPONIN C (81- 161) BOUND TO THE N TERMINAL DOMAIN OF CARDIAC TROPONIN I (33-80), CALCIUM IONS BOUND AT SITES III AND IV
Cell: MYOCYTE / Cellular location: THIN FILAMENT / Organ: HEART / Plasmid: PET-23D+ / Species (production host): Escherichia coli / Gene (production host): CTNC(81-161) / 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
12115N-NOESY- HSQC
13115N-TOCSY-HSQC
141HNCO
151HN(CA)CB
161(HB)CBCA (CO)NNH
171H(CCO)NH
181C (CO)NH
191(HB)CB(CGCD)HD
1101(HB)CB(CGCDCE)HE
1111CN- NOESY-HSQC
1121HNHA
1131HNHB.
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, 100mM KCL,15mM CACL2 / pH: 6.80 / Pressure: ambient / Temperature: 318.00 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian INOVA600VarianINOVA6006001
Varian INOVA800VarianINOVA8008002

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Processing

NMR software
NameVersionDeveloperClassification
CNS1BRUNGERrefinement
CNS1BRUNGERstructure solution
RefinementMethod: DGSA / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: SMALLEST RMSD TO AVERAGE STRUCTURE
Conformers calculated total number: 500 / Conformers submitted total number: 20

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