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- PDB-1blq: STRUCTURE AND INTERACTION SITE OF THE REGULATORY DOMAIN OF TROPON... -

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Basic information

Entry
Database: PDB / ID: 1blq
TitleSTRUCTURE AND INTERACTION SITE OF THE REGULATORY DOMAIN OF TROPONIN-C WHEN COMPLEXED WITH THE 96-148 REGION OF TROPONIN-I, NMR, 29 STRUCTURES
ComponentsN-TROPONIN C
KeywordsCALCIUM-BINDING PROTEIN / CALCIUM-BINDING / REGULATION / TROPONIN C / SKELETAL MUSCLE / CONTRACTION
Function / homology
Function and homology information


troponin complex / Striated Muscle Contraction / skeletal muscle contraction / calcium ion binding
Similarity search - Function
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 / simulated annealing
AuthorsMckay, R.T. / Pearlstone, J.R. / Corson, D.C. / Gagne, S.M. / Smillie, L.B. / Sykes, B.D.
CitationJournal: Biochemistry / Year: 1998
Title: Structure and interaction site of the regulatory domain of troponin-C when complexed with the 96-148 region of troponin-I.
Authors: McKay, R.T. / Pearlstone, J.R. / Corson, D.C. / Gagne, S.M. / Smillie, L.B. / Sykes, B.D.
History
DepositionJul 19, 1998Processing site: BNL
Revision 1.0Jan 13, 1999Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: N-TROPONIN C


Theoretical massNumber of molelcules
Total (without water)9,9841
Polymers9,9841
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)29 / 30LEAST RESTRAINT VIOLATION
RepresentativeModel #3

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Components

#1: Protein N-TROPONIN C / SNTNC


Mass: 9984.085 Da / Num. of mol.: 1 / Fragment: REGULATORY
Source method: isolated from a genetically manipulated source
Details: COMPLEX OF SNTNC WITH TNI PEPTIDE / Source: (gene. exp.) Gallus gallus (chicken) / Tissue: SKELETAL MUSCLE / Cell line: BL21 / Organ: SKELETALSkeleton / Plasmid: PET3A / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) PLYSS / References: UniProt: P02588

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
11115N-HMQC
12115N-HSQC
131TOCSY-HMQC
141(H)CCH-TOCSY
151CBCA(CO)NNH
16115N-NOESYHSQC
17115N-NOESYHMQC
18113C15N-NOESY
191HNCO
1101HNCA
1111HCACO
1121FILTER/ EDIT NOESY
1131EDIT/FILTER NOESY
NMR detailsText: MODEL 3 STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED CALCIUM-SATURATED CHICKEN SKELETAL TROPONIN-C WHILE COMPLEXED WITH A TROPONIN-I PEPTIDE OF RESIDUES ...Text: MODEL 3 STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED CALCIUM-SATURATED CHICKEN SKELETAL TROPONIN-C WHILE COMPLEXED WITH A TROPONIN-I PEPTIDE OF RESIDUES 96-148. THE SITE OF INTERACTION WAS ALSO DETERMINED.

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Sample preparation

DetailsContents: H2O
Sample conditionsIonic strength: 100 mM KCL / pH: 6.85 / Pressure: 1 atm / Temperature: 303 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian UNITY INOVAVarianUNITY INOVA5001
Varian UNITYVarianUNITY6002

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Processing

Software
NameVersionClassification
X-PLOR3.851model building
X-PLOR3.851refinement
X-PLOR3.851phasing
NMR software
NameVersionDeveloperClassification
X-PLOR3.851BRUNGERrefinement
X-PLORstructure solution
RefinementMethod: simulated annealing / 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: 30 / Conformers submitted total number: 29

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