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- PDB-1cmf: NMR SOLUTION STRUCTURE OF APO CALMODULIN CARBOXY-TERMINAL DOMAIN -

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Basic information

Entry
Database: PDB / ID: 1cmf
TitleNMR SOLUTION STRUCTURE OF APO CALMODULIN CARBOXY-TERMINAL DOMAIN
ComponentsCALMODULIN (VERTEBRATE)
KeywordsCALCIUM-BINDING PROTEIN
Function / homology
Function and homology information


positive regulation of ryanodine-sensitive calcium-release channel activity / negative regulation of ryanodine-sensitive calcium-release channel activity / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / spindle pole / protein domain specific binding / calcium ion binding / protein-containing complex / cytosol / cytoplasm
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 ...: / 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
Biological speciesBos taurus (cattle)
MethodSOLUTION NMR
AuthorsFinn, B.E. / Evenas, J. / Drakenberg, T. / Waltho, J.P. / Thulin, E. / Forsen, S.
Citation
Journal: Nat.Struct.Biol. / Year: 1995
Title: Calcium-induced structural changes and domain autonomy in calmodulin.
Authors: Finn, B.E. / Evenas, J. / Drakenberg, T. / Waltho, J.P. / Thulin, E. / Forsen, S.
#1: Journal: FEBS Lett. / Year: 1993
Title: The Structure of Apo-Calmodulin: A 1H NMR Examination of Carboxy-Terminal Domain
Authors: Finn, B.E. / Drakenberg, T. / Forsen, S.
History
DepositionJul 19, 1995Processing site: BNL
Revision 1.0Dec 7, 1995Provider: repository / Type: Initial release
Revision 1.1Mar 3, 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
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: CALMODULIN (VERTEBRATE)


Theoretical massNumber of molelcules
Total (without water)8,4161
Polymers8,4161
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)20 / -
Representative

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Components

#1: Protein CALMODULIN (VERTEBRATE) / CALMODULIN APO TR2C-DOMAIN


Mass: 8416.203 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (cattle) / Organ: BRAIN / Plasmid: PRCB1 / Production host: Escherichia coli (E. coli) / References: UniProt: P62157

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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

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR softwareName: X-PLOR / Version: 3.1 / Developer: BRUNGER / Classification: refinement
NMR ensembleConformers submitted total number: 20

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