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- PDB-1ncu: Titin Module M5, N-terminally Extended, NMR -

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Basic information

Entry
Database: PDB / ID: 1ncu
TitleTitin Module M5, N-terminally Extended, NMR
ComponentsTITIN
KeywordsMUSCLE PROTEIN / CELL ADHESION / GLYCOPROTEIN / TRANSMEMBRANE / BRAIN / IMMUNOGLOBULIN FOLD / ALTERNATIVE SPLICING
Function / homology
Function and homology information


sarcomerogenesis / structural molecule activity conferring elasticity / telethonin binding / skeletal muscle myosin thick filament assembly / cardiac myofibril assembly / detection of muscle stretch / muscle alpha-actinin binding / cardiac muscle tissue morphogenesis / regulation of catalytic activity / Striated Muscle Contraction ...sarcomerogenesis / structural molecule activity conferring elasticity / telethonin binding / skeletal muscle myosin thick filament assembly / cardiac myofibril assembly / detection of muscle stretch / muscle alpha-actinin binding / cardiac muscle tissue morphogenesis / regulation of catalytic activity / Striated Muscle Contraction / mitotic chromosome condensation / cardiac muscle hypertrophy / M band / actinin binding / I band / cardiac muscle cell development / regulation of protein kinase activity / structural constituent of muscle / sarcomere organization / 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 / 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
AuthorsPfuhl, M. / Pastore, A.
Citation
Journal: J.Mol.Biol. / Year: 1997
Title: When a module is also a domain: the role of the N terminus in the stability and the dynamics of immunoglobulin domains from titin.
Authors: Pfuhl, M. / Improta, S. / Politous, A.S. / Pastore, A.
#1: Journal: Structure / Year: 1996
Title: Immunoglobulin-Like Modules from Titin I-Band Extensible Components of Muscle Elasticity
Authors: Improta, S. / Politou, A.S. / Pastore, A.
#2: Journal: Structure / Year: 1995
Title: Tertiary Structure of an Immunoglobulin-Like Domain from the Giant Muscle Protein Titin: A New Member of the I Set
Authors: Pfuhl, M. / Pastore, A.
#3: Journal: J.Biomol.NMR / Year: 1995
Title: Secondary Structure Determination by NMR Spectroscopy of an Immunoglobulin-Like Domain from the Giant Muscle Protein Titin
Authors: Pfuhl, M. / Gautel, M. / Politou, A.S. / Joseph, C. / Pastore, A.
#4: Journal: FEBS Lett. / Year: 1994
Title: Immunoglobulin-Type Domains of Titin are Stabilized by Amino-Terminal Extension
Authors: Politou, A.S. / Gautel, M. / Joseph, C. / Pastore, A.
History
DepositionAug 13, 1996Processing site: BNL
Revision 1.0Nov 8, 1996Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_assembly ...pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conf
Item: _pdbx_database_status.process_site

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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)11,8821
Polymers11,8821
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)16 / -
Representative

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Components

#1: Protein TITIN / / CONNECTIN / NEXTM5


Mass: 11882.170 Da / Num. of mol.: 1 / Fragment: N-TERMINALLY EXTENDED MODULE M5
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Tissue: CARDIAC MUSCLE / Cell line: BL21 / Organelle: CYTOPLASMA/SARCOMERE / Plasmid: PET8C / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 PLYS / References: UniProt: Q10466, UniProt: Q8WZ42*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR detailsText: 20 MM ACETATE BUFFER, NO OTHER SALTS

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Sample preparation

Sample conditionspH: 4.8 / Temperature: 300 K
Crystal grow
*PLUS
Method: other / Details: NMR

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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: 16

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