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- PDB-1h67: NMR Structure of the CH Domain of Calponin -

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Basic information

Entry
Database: PDB / ID: 1h67
TitleNMR Structure of the CH Domain of Calponin
ComponentsCALPONIN ALPHA
KeywordsCYTOSKELETON / CALPONIN HOMOLOGY DOMAIN / ACTIN BINDING
Function / homology
Function and homology information


actin crosslink formation / cytoskeletal anchor activity / actomyosin structure organization / actin filament / microtubule cytoskeleton organization / actin filament binding / microtubule binding / microtubule / calmodulin binding
Similarity search - Function
Calponin/LIMCH1 / Calponin repeat / Calponin family repeat / Calponin-like repeat signature. / Calponin-like repeat profile. / Smooth muscle protein/calponin / Calponin-like domain / Actin-binding Protein, T-fimbrin; domain 1 / Calponin homology domain / Calponin homology (CH) domain ...Calponin/LIMCH1 / Calponin repeat / Calponin family repeat / Calponin-like repeat signature. / Calponin-like repeat profile. / Smooth muscle protein/calponin / Calponin-like domain / Actin-binding Protein, T-fimbrin; domain 1 / Calponin homology domain / Calponin homology (CH) domain / Calponin homology domain / CH domain superfamily / Calponin homology (CH) domain profile. / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Calponin-1 / Calponin-1
Similarity search - Component
Biological speciesGALLUS GALLUS (chicken)
MethodSOLUTION NMR / simulated annealing
AuthorsBramham, J. / Smith, B.O. / Uhrin, D. / Barlow, P.N. / Winder, S.J.
CitationJournal: Structure / Year: 2002
Title: Solution Structure of the Calponin Ch Domain and Fitting to the 3D-Helical Reconstruction of F-Actin:Calponin.
Authors: Bramham, J. / Hodgkinson, J.L. / Smith, B.O. / Uhrin, D. / Barlow, P.N. / Winder, S.J.
History
DepositionJun 7, 2001Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 14, 2002Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jan 15, 2020Group: Data collection / Other / Category: pdbx_database_status / pdbx_nmr_software
Item: _pdbx_database_status.status_code_cs / _pdbx_nmr_software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: CALPONIN ALPHA


Theoretical massNumber of molelcules
Total (without water)12,2671
Polymers12,2671
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)20 / 50LEAST RESTRAINT VIOLATION
RepresentativeModel #9

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Components

#1: Protein CALPONIN ALPHA


Mass: 12266.951 Da / Num. of mol.: 1 / Fragment: CALPONIN HOMOLOGY DOMAIN, RESIDUES 28-134
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) GALLUS GALLUS (chicken) / Tissue: SMOOTH MUSCLE / Organ: GIZZARD / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q9PSG0, UniProt: P26932*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
11113C
12115N HSQC-NOESY-CH3NH
13113C-EDITTED NOESY-HSQC
NMR detailsText: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED PROTEIN.

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Sample preparation

DetailsContents: 1MM CALPONIN CH DOMAIN
Sample conditionsIonic strength: 0 / pH: 7.0 / Temperature: 291 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz

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Processing

NMR software
NameDeveloperClassification
CNSA.T.BRUNGER,P.D.ADAMS, G.M.CLORE,W.L.DELANO, P.GROS, R.W.GROSSE-KUNSTLEVE,J.-S.JIANG, J.KUSZEWSKI,M.NILGES,N.S.PANNU, R.J.READ, L.M.RICE,T.SIMONSON,G.L.WARRENrefinement
Azarastructure solution
ANSIGstructure solution
CNSstructure 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: 50 / Conformers submitted total number: 20

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