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- PDB-7nip: titin N2A unique sequence (UN2A) core -

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Basic information

Entry
Database: PDB / ID: 7nip
Titletitin N2A unique sequence (UN2A) core
ComponentsIsoform 11 of Titin
KeywordsSTRUCTURAL PROTEIN / titin / N2A / UN2A
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 / regulation of catalytic 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 / regulation of catalytic activity / cardiac muscle hypertrophy / mitotic chromosome condensation / Striated Muscle Contraction / M band / actinin binding / I band / cardiac muscle cell development / regulation of protein kinase activity / sarcomere organization / structural constituent of muscle / skeletal muscle thin filament assembly / striated muscle thin filament / striated muscle contraction / protein kinase A signaling / cardiac muscle contraction / muscle contraction / condensed nuclear chromosome / positive regulation of protein secretion / Z disc / response to calcium ion / : / actin filament binding / Platelet degranulation / protein tyrosine kinase activity / protease binding / calmodulin binding / non-specific serine/threonine protein kinase / phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / calcium ion binding / positive regulation of gene expression / protein kinase binding / enzyme binding / 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 / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / na
AuthorsZhou, T. / Kovermann, M. / Fleming, J.R. / Mayans, O.
Funding support France, European Union, 2items
OrganizationGrant numberCountry
Leducq FoundationTNE-13CVD04 France
H2020 Marie Curie Actions of the European Commission753054European Union
CitationJournal: J.Mol.Biol. / Year: 2021
Title: Molecular Characterisation of Titin N2A and Its Binding of CARP Reveals a Titin/Actin Cross-linking Mechanism.
Authors: Zhou, T. / Fleming, J.R. / Lange, S. / Hessel, A.L. / Bogomolovas, J. / Stronczek, C. / Grundei, D. / Ghassemian, M. / Biju, A. / Borgeson, E. / Bullard, B. / Linke, W.A. / Chen, J. / Kovermann, M. / Mayans, O.
History
DepositionFeb 13, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 3, 2021Provider: repository / Type: Initial release
Revision 1.1Mar 17, 2021Group: Database references / Category: citation / citation_author
Item: _citation.page_first / _citation.page_last ..._citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name
Revision 1.2Mar 31, 2021Group: Database references / Category: citation / Item: _citation.journal_volume / _citation.title

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Isoform 11 of Titin


Theoretical massNumber of molelcules
Total (without water)4,9331
Polymers4,9331
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area0 Å2
ΔGint0 kcal/mol
Surface area3290 Å2
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 32500all calculated structures submitted
RepresentativeModel #1closest to the average

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Components

#1: Protein/peptide Isoform 11 of Titin / Connectin / Rhabdomyosarcoma antigen MU-RMS-40.14


Mass: 4932.733 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TTN / Production host: Escherichia coli (E. coli)
References: UniProt: Q8WZ42, non-specific serine/threonine protein kinase

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
111isotropic13D HNCO
121isotropic13D HNCA
131isotropic13D HN(CA)CB
141isotropic13D HN(COCA)CB
151isotropic12D 1H-15N HSQC

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Sample preparation

DetailsType: solution
Contents: 30 mM sodium phosphate, 100 mM sodium chloride, 95% H2O/5% D2O
Label: sample_un2a / Solvent system: 95% H2O/5% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
30 mMsodium phosphatenatural abundance1
100 mMsodium chloridenatural abundance1
Sample conditionsIonic strength: 100 mM / Label: conditions_1 / pH: 7.5 / Pressure: 101300 Pa / Temperature: 298 K

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NMR measurement

NMR spectrometerType: Bruker AVANCE III / Manufacturer: Bruker / Model: AVANCE III / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
TALOSCornilescu, Delaglio and Baxchemical shift assignment
CS-ROSETTAShen, Vernon, Baker and Baxstructure calculation
NMRViewJ8.0.a27One Moon Scientificchemical shift assignment
RefinementMethod: na / Software ordinal: 1
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: all calculated structures submitted
Conformers calculated total number: 32500 / Conformers submitted total number: 10

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