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- PDB-1owa: Solution Structural Studies on Human Erythrocyte Alpha Spectrin N... -

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Basic information

Entry
Database: PDB / ID: 1owa
TitleSolution Structural Studies on Human Erythrocyte Alpha Spectrin N Terminal Tetramerization Domain
ComponentsSpectrin alpha chain, erythrocyte
KeywordsCYTOKINE / triple helical bundle
Function / homology
Function and homology information


cuticular plate / spectrin / lymphocyte homeostasis / spectrin-associated cytoskeleton / porphyrin-containing compound biosynthetic process / plasma membrane organization / actin filament capping / Interaction between L1 and Ankyrins / cortical actin cytoskeleton / hemopoiesis ...cuticular plate / spectrin / lymphocyte homeostasis / spectrin-associated cytoskeleton / porphyrin-containing compound biosynthetic process / plasma membrane organization / actin filament capping / Interaction between L1 and Ankyrins / cortical actin cytoskeleton / hemopoiesis / COPI-mediated anterograde transport / positive regulation of T cell proliferation / NCAM signaling for neurite out-growth / actin filament organization / cell projection / cytoplasmic side of plasma membrane / structural constituent of cytoskeleton / actin filament binding / actin cytoskeleton / cell junction / regulation of cell shape / actin cytoskeleton organization / RAF/MAP kinase cascade / axon / calcium ion binding / plasma membrane / cytosol
Similarity search - Function
Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #60 / EF-hand, Ca insensitive / Ca2+ insensitive EF hand / Ca2+ insensitive EF hand / Spectrin repeat / Spectrin repeat / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #170 / Spectrin/alpha-actinin / Spectrin repeats / Methane Monooxygenase Hydroxylase; Chain G, domain 1 ...Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #60 / EF-hand, Ca insensitive / Ca2+ insensitive EF hand / Ca2+ insensitive EF hand / Spectrin repeat / Spectrin repeat / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #170 / Spectrin/alpha-actinin / Spectrin repeats / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / SH3 domain / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Src homology 3 domains / EF-hand calcium-binding domain profile. / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / EF-hand domain / EF-hand domain pair / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Spectrin alpha chain, erythrocytic 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / torsion angle dynamics
AuthorsPark, S. / Caffrey, M.S. / Johnson, M.E. / Fung, L.W.
CitationJournal: J.Biol.Chem. / Year: 2003
Title: Solution structural studies on human erythrocyte alpha-spectrin tetramerization site.
Authors: Park, S. / Caffrey, M.S. / Johnson, M.E. / Fung, L.W.
History
DepositionMar 28, 2003Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 30, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 29, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
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: Spectrin alpha chain, erythrocyte


Theoretical massNumber of molelcules
Total (without water)18,5601
Polymers18,5601
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)10 / 200Lowest Energy conformers
RepresentativeModel #1lowest energy

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Components

#1: Protein Spectrin alpha chain, erythrocyte / Erythroid alpha-spectrin


Mass: 18559.852 Da / Num. of mol.: 1 / Fragment: residues 1-156
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SPTA1 / Production host: Escherichia coli (E. coli) / References: UniProt: P02549

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
1212D TOCSY
1313D 13C-separated NOESY
1413D 15N-separated NOESY
1514D 13C-separated NOESY

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Sample preparation

DetailsContents: 1mM spectrin, 5mM Phosphate, 150mM NaCl, 5% D2O, 95 % H2O
Solvent system: 5% D2O, 95 % H2O
Sample conditionsIonic strength: 5mM Phosphate, 150mM NaCl / pH: 6.5 / Pressure: ambient / Temperature: 293 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX6001
Bruker DMXBrukerDMX7502

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Processing

NMR software
NameVersionDeveloperClassification
CNS1.1Brungerstructure solution
CNS1.1Brungerrefinement
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: Lowest Energy conformers / Conformers calculated total number: 200 / Conformers submitted total number: 10

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