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- PDB-1skt: SOLUTION STRUCTURE OF APO N-DOMAIN OF TROPONIN C, NMR, 40 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 1skt
TitleSOLUTION STRUCTURE OF APO N-DOMAIN OF TROPONIN C, NMR, 40 STRUCTURES
ComponentsTROPONIN-C
KeywordsCALCIUM-BINDING PROTEIN / EF-HAND / LOW-TEMPERATURE
Function / homology
Function and homology information


troponin complex / Striated Muscle Contraction / skeletal muscle contraction / 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 / 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, skeletal muscle
Similarity search - Component
Biological speciesGallus gallus (chicken)
MethodSOLUTION NMR / DISGEO,SA
AuthorsTsuda, S. / Miura, A. / Gagne, S.M. / Spyracopoulos, L. / Sykes, B.D.
Citation
Journal: Biochemistry / Year: 1999
Title: Low-temperature-induced structural changes in the Apo regulatory domain of skeletal muscle troponin C.
Authors: Tsuda, S. / Miura, A. / Gagne, S.M. / Spyracopoulos, L. / Sykes, B.D.
#1: Journal: To be Published
Title: Low Temperature Effect on Dynamics of Apo N-Domain of Troponin C
Authors: Tsuda, S. / Gagne, S.M. / Spyracopoulos, L. / Sykes, B.D.
History
DepositionApr 6, 1998Processing site: BNL
Revision 1.0Dec 9, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Experimental preparation / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_exptl_sample_conditions / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_nmr_exptl_sample_conditions.pressure_units / _pdbx_nmr_software.name
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


Theoretical massNumber of molelcules
Total (without water)9,9841
Polymers9,9841
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)40 / 100LEAST RESTRAINT VIOLATION
Representative

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Components

#1: Protein TROPONIN-C / NTNC APO


Mass: 9984.085 Da / Num. of mol.: 1 / Fragment: N-DOMAIN, RESIDUES 1-90
Source method: isolated from a genetically manipulated source
Details: RESIDUES 1-90 OF CHICKEN SKELETAL MUSCLE TROPONIN C IN CA2+-FREE STATE
Source: (gene. exp.) Gallus gallus (chicken) / Tissue: SKELETON / Gene: NTNC / Organ: SKELETAL / Plasmid: PET3A / Gene (production host): NTNC / Production host: Escherichia coli (E. coli) / References: UniProt: P02588

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111CBCACONNH
12115N-NOESY
131HNHA
NMR detailsText: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C,15N-LABELED APO NTNC.

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Sample preparation

DetailsContents: WATER
Sample conditionsIonic strength: 50mM KCL / pH: 6.7 / Pressure: 1 atm / Temperature: 277 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian UNITY500VarianUNITY5005001
Varian 600Varian6006002

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Processing

Software
NameVersionClassification
X-PLOR3.851model building
X-PLOR3.851refinement
X-PLOR3.851phasing
NMR software
NameVersionDeveloperClassification
X-PLOR3.851BRUNGERrefinement
NMRPipestructure solution
PIPPstructure solution
RefinementMethod: DISGEO,SA / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE.
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 100 / Conformers submitted total number: 40

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