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- PDB-1bpv: TITIN MODULE A71 FROM HUMAN CARDIAC MUSCLE, NMR, 50 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 1bpv
TitleTITIN MODULE A71 FROM HUMAN CARDIAC MUSCLE, NMR, 50 STRUCTURES
ComponentsTITIN
KeywordsCONNECTIN / TITIN / FIBRONECTIN TYPE III
Function / homology
Function and homology information


sarcomerogenesis / structural molecule activity conferring elasticity / telethonin binding / skeletal muscle myosin thick filament assembly / cardiac myofibril assembly / muscle alpha-actinin binding / detection of muscle stretch / cardiac muscle tissue morphogenesis / protein kinase regulator activity / cardiac muscle hypertrophy ...sarcomerogenesis / structural molecule activity conferring elasticity / telethonin binding / skeletal muscle myosin thick filament assembly / cardiac myofibril assembly / muscle alpha-actinin binding / detection of muscle stretch / cardiac muscle tissue morphogenesis / protein kinase regulator activity / cardiac muscle hypertrophy / mitotic chromosome condensation / actinin binding / Striated Muscle Contraction / M band / I band / cardiac muscle cell development / structural constituent of muscle / sarcomere organization / skeletal muscle thin filament assembly / striated muscle thin filament / cardiac muscle contraction / striated muscle contraction / muscle contraction / protein kinase A signaling / condensed nuclear chromosome / positive regulation of protein secretion / Z disc / response to calcium ion / actin filament binding / Platelet degranulation / protease binding / protein tyrosine kinase activity / calmodulin binding / non-specific serine/threonine protein kinase / protein serine kinase activity / protein serine/threonine kinase activity / calcium ion binding / positive regulation of gene expression / protein kinase binding / enzyme binding / protein homodimerization activity / extracellular exosome / extracellular region / ATP binding / identical protein binding / cytosol
Similarity search - Function
PPAK motif / PPAK motif / Titin, Z repeat / Titin Z / 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 ...PPAK motif / PPAK motif / Titin, Z repeat / Titin Z / 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 / Immunoglobulin V-Type / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin V-set domain / Immunoglobulin subtype / Immunoglobulin / Tyrosine-protein kinase, active site / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Protein kinase domain / Immunoglobulins / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
AuthorsMuhle-Goll, C. / Pastore, A. / Nilges, M.
CitationJournal: Structure / Year: 1998
Title: The three-dimensional structure of a type I module from titin: a prototype of intracellular fibronectin type III domains.
Authors: Goll, C.M. / Pastore, A. / Nilges, M.
History
DepositionAug 11, 1998Processing site: BNL
Revision 1.0Aug 12, 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
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: TITIN


Theoretical massNumber of molelcules
Total (without water)12,4771
Polymers12,4771
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)50 / 1LEAST RESTRAINT VIOLATION
RepresentativeModel #1

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Components

#1: Protein TITIN / A71 / CONNECTIN


Mass: 12476.979 Da / Num. of mol.: 1 / Fragment: 71 TH DOMAIN FROM THE A-BAND / Mutation: I9V
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Tissue: MUSCLE / Organ: HEART / Organelle: SARCOMERE / Plasmid: PET8C / Gene (production host): TITIN GENE / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 PLYSS / References: UniProt: Q10466, UniProt: Q8WZ42*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121TOCSY
131HSQC
1413D NOESY-HSQC
NMR detailsText: REPRESENTATIVE MODEL NUMBER: 1 THE STRUCTURE WAS DETERMINED USING A 3D N15-EDITED NOESY-HSQC AND HOMONUCLEAR 2D NOESY EXPERIMENTS.

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Sample preparation

DetailsContents: 10 MM ACETATE BUFFER
Sample conditionsIonic strength: 50 mM NACL / pH: 5.6 / Temperature: 310 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker AMX600 / Manufacturer: Bruker / Model: AMX600 / Field strength: 600 MHz

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Processing

Software
NameClassification
X-PLORmodel building
X-PLORrefinement
X-PLORphasing
NMR software
NameVersionDeveloperClassification
XPLOR 3.851 (EXTENDED VERSION)VERSION)BRUNGER, NILGESrefinement
XPLOR (EXTENDED VERSION)VERSION)structure solution
RefinementMethod: simulated annealing / Software ordinal: 1
Details: STRUCTURE CALCULATIONS WERE PERFORMED WITH THE SUPPORT OF THE ARIA (AMBIGUOUS RESTRAINTS FOR ITERATIVE ASSIGNMENT) PROTOCOL (NILGES ET AL., J. MOL. BIOL. 269, 408-422). 100 STRUCTURES WERE ...Details: STRUCTURE CALCULATIONS WERE PERFORMED WITH THE SUPPORT OF THE ARIA (AMBIGUOUS RESTRAINTS FOR ITERATIVE ASSIGNMENT) PROTOCOL (NILGES ET AL., J. MOL. BIOL. 269, 408-422). 100 STRUCTURES WERE CALCULATED OF WHICH THE BEST 50 STRUCTURES WERE SELECTED.
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 1 / Conformers submitted total number: 50

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