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- PDB-1gxe: Central domain of cardiac myosin binding protein C -

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Basic information

Entry
Database: PDB / ID: 1gxe
TitleCentral domain of cardiac myosin binding protein C
ComponentsMYOSIN BINDING PROTEIN C, CARDIAC-TYPE
KeywordsCYTOSKELETON / MUSCLE / IGI / THICK FILAMENT / IMMUNOGLOBULIN DOMAIN
Function / homology
Function and homology information


C zone / regulation of muscle filament sliding / striated muscle myosin thick filament / cardiac myofibril / regulation of striated muscle contraction / positive regulation of ATP-dependent activity / Striated Muscle Contraction / A band / ventricular cardiac muscle tissue morphogenesis / structural constituent of muscle ...C zone / regulation of muscle filament sliding / striated muscle myosin thick filament / cardiac myofibril / regulation of striated muscle contraction / positive regulation of ATP-dependent activity / Striated Muscle Contraction / A band / ventricular cardiac muscle tissue morphogenesis / structural constituent of muscle / myosin binding / sarcomere organization / myosin heavy chain binding / ATPase activator activity / heart morphogenesis / cardiac muscle contraction / titin binding / sarcomere / actin binding / cell adhesion / identical protein binding / metal ion binding / cytosol
Similarity search - Function
MyBP-C, tri-helix bundle domain / Tri-helix bundle domain / Immunoglobulin I-set / Immunoglobulin I-set domain / Fibronectin type III domain / Fibronectin type 3 domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Fibronectin type-III domain profile. / Fibronectin type III ...MyBP-C, tri-helix bundle domain / Tri-helix bundle domain / Immunoglobulin I-set / Immunoglobulin I-set domain / Fibronectin type III domain / Fibronectin type 3 domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulins / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Myosin-binding protein C, cardiac-type
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodSOLUTION NMR / simulated annealing
AuthorsPfuhl, M.
Citation
Journal: J.Mol.Biol. / Year: 2003
Title: Structure, Stability and Dynamics of the Central Domain of Cardiac Myosin Binding Protein C (Mybp-C): Implications for Multidomain Assembly and Causes for Cardiomyopathy
Authors: Idowu, S. / Gautel, M. / Perkins, S. / Pfuhl, M.
#1: Journal: J.Biomol.NMR / Year: 2002
Title: Sequence Specific Resonance Assignment of the Central Domain of Cardiac Myosin Binding Protein C (Mybp-C)
Authors: Idowu, S. / Gautel, M. / Pfuhl, M.
History
DepositionApr 3, 2002Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 12, 2003Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 28, 2018Group: Data collection / Source and taxonomy / Structure summary
Category: entity_src_gen / pdbx_nmr_software / struct
Item: _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id / _entity_src_gen.pdbx_host_org_scientific_name ..._entity_src_gen.pdbx_host_org_ncbi_taxonomy_id / _entity_src_gen.pdbx_host_org_scientific_name / _entity_src_gen.pdbx_host_org_strain / _entity_src_gen.pdbx_host_org_variant / _pdbx_nmr_software.name / _struct.title
Revision 1.4May 15, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_nmr_software
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_mr / _pdbx_nmr_software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: MYOSIN BINDING PROTEIN C, CARDIAC-TYPE


Theoretical massNumber of molelcules
Total (without water)15,3951
Polymers15,3951
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)10 / 200RESTRAINT VIOLATIONS 0.2 A
RepresentativeModel #1

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Components

#1: Protein MYOSIN BINDING PROTEIN C, CARDIAC-TYPE / CARDIAC MYBP-C / C-PROTEIN - CARDIAC MUSCLE ISOFORM


Mass: 15395.244 Da / Num. of mol.: 1 / Fragment: DOMAIN C5, RESIDUES 641-770
Source method: isolated from a genetically manipulated source
Details: HIS-TAGGED PROTEIN / Source: (gene. exp.) HOMO SAPIENS (human) / Tissue: MUSCLE / Description: CARDIAC PROTEIN / Cell: MYOCYTE / Organ: HEART / Plasmid: PET8C / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q14896

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
11115N NOESY-HSQC
12113C NOESY-HSQC
NMR detailsText: 3D 15N NOESY-HSQC & 3D 13C NOESY-HSQC IN 90% H2O/10% D2O 3D 13C NOESY-HSQC IN 99% D2O

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Sample preparation

Sample conditionsIonic strength: 100 MM NACL / pH: 7.0 / Pressure: 1 atm / Temperature: 293 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

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

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
X-PLORstructure solution
RefinementMethod: simulated annealing / Software ordinal: 1
Details: SIMULATED ANNEALING WITH STANDARD XPLOR PROTOCOL DESCRIBED IN MANUSCRIPT. RESIDUES -9 TO -1 CONSTITUTE A HIS-TAG. THESE RESIDUES WERE PRESENT IN THE EXPERIMENT BUT WERE NOT ASSIGNED NOR USED ...Details: SIMULATED ANNEALING WITH STANDARD XPLOR PROTOCOL DESCRIBED IN MANUSCRIPT. RESIDUES -9 TO -1 CONSTITUTE A HIS-TAG. THESE RESIDUES WERE PRESENT IN THE EXPERIMENT BUT WERE NOT ASSIGNED NOR USED IN THE STRUCTURE CALCULATION.
NMR ensembleConformer selection criteria: RESTRAINT VIOLATIONS 0.2 A / Conformers calculated total number: 200 / Conformers submitted total number: 10

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