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- PDB-1pon: SITE III-SITE IV TROPONIN C HETERODIMER, NMR -

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Basic information

Entry
Database: PDB / ID: 1pon
TitleSITE III-SITE IV TROPONIN C HETERODIMER, NMR
Components(TROPONIN C) x 2
KeywordsCALCIUM-BINDING PROTEIN / EF-HAND / MUSCLE PROTEIN
Function / homology
Function and homology information


Striated Muscle Contraction / troponin complex / skeletal muscle contraction / calcium ion binding
Similarity search - Function
: / 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
Similarity search - Domain/homology
Troponin C, skeletal muscle
Similarity search - Component
Biological speciesGallus gallus (chicken)
MethodSOLUTION NMR
AuthorsShaw, G.S. / Sykes, B.D.
Citation
Journal: Biochemistry / Year: 1996
Title: NMR solution structure of a synthetic troponin C heterodimeric domain.
Authors: Shaw, G.S. / Sykes, B.D.
#1: Journal: To be Published
Title: Relative Stabilities of Synthetic Peptide Homo-and Heterodimeric Troponin-C Domains Journal Title: Protein Science
Authors: Shaw, G.S. / Hodges, R.S. / Kay, C.M. / Sykes, B.D.
History
DepositionApr 2, 1996Processing site: BNL
Revision 1.0Nov 8, 1996Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 3, 2021Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_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_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Oct 9, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: TROPONIN C
B: TROPONIN C


Theoretical massNumber of molelcules
Total (without water)7,8922
Polymers7,8922
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)42 / -
Representative

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Components

#1: Protein/peptide TROPONIN C


Mass: 3856.234 Da / Num. of mol.: 1 / Fragment: SITE III AND IV
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / References: UniProt: P02588
#2: Protein/peptide TROPONIN C


Mass: 4035.425 Da / Num. of mol.: 1 / Fragment: SITE III AND IV
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / References: UniProt: P02588
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

NMR softwareName: DGII / Developer: HAVEL / Classification: refinement
NMR ensembleConformers submitted total number: 42

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