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- PDB-1aj3: SOLUTION STRUCTURE OF THE SPECTRIN REPEAT, NMR, 20 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 1aj3
TitleSOLUTION STRUCTURE OF THE SPECTRIN REPEAT, NMR, 20 STRUCTURES
ComponentsALPHA SPECTRIN
KeywordsCYTOSKELETON / ELASTICITY / MEMBRANE SKELETON / SPECTRIN / COILED-COIL / CALMODULIN-BINDING / ACTIN-BINDING / CAPPING PROTEIN / CALCIUM-BINDING / DUPLICATION / SH3 DOMAIN
Function / homology
Function and homology information


actin filament capping / costamere / cortical actin cytoskeleton / cell projection / actin filament binding / cell junction / actin cytoskeleton organization / calmodulin binding / calcium ion binding / plasma membrane
Similarity search - Function
Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #60 / Alpha Spectrin, SH3 domain / EF-hand, Ca insensitive / Ca2+ insensitive EF hand / Ca2+ insensitive EF hand / Spectrin repeat / Spectrin repeat / Spectrin/alpha-actinin / Spectrin repeats / Methane Monooxygenase Hydroxylase; Chain G, domain 1 ...Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #60 / Alpha Spectrin, SH3 domain / EF-hand, Ca insensitive / Ca2+ insensitive EF hand / Ca2+ insensitive EF hand / Spectrin repeat / Spectrin repeat / Spectrin/alpha-actinin / Spectrin repeats / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / SH3 domain / EF-hand domain pair / EF-hand, calcium binding motif / Src homology 3 domains / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / 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, non-erythrocytic 1
Similarity search - Component
Biological speciesGallus gallus (chicken)
MethodSOLUTION NMR / molecular dynamics
AuthorsPascual, J. / Pfuhl, M. / Walther, D. / Saraste, M. / Nilges, M.
CitationJournal: J.Mol.Biol. / Year: 1997
Title: Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil.
Authors: Pascual, J. / Pfuhl, M. / Walther, D. / Saraste, M. / Nilges, M.
History
DepositionMay 14, 1997Processing site: BNL
Revision 1.0Jul 7, 1997Provider: 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: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_nmr_software.name
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: ALPHA SPECTRIN


Theoretical massNumber of molelcules
Total (without water)12,8281
Polymers12,8281
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)20 / 40ENERGY, GEOMETRY, VIOLATIONS
Representative

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Components

#1: Protein ALPHA SPECTRIN


Mass: 12828.446 Da / Num. of mol.: 1 / Fragment: 16TH REPEAT, RESIDUES 1772 - 1869
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / Cell line: BL21 / Organ: BRAIN / Plasmid: PET-3D / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P07751

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111HNCA
121HN(CO)CA
131HNCO
141HN (CA)CO
151(H)CCH-COSY
161(H)CCH-TOCSY
17115N
18113C HSQC-NOESY

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Sample preparation

Sample conditionspH: 6 / Temperature: 308 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DMXBrukerDMX5001
Bruker DMXBrukerDMX6002

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR software
NameVersionDeveloperClassification
X-PLOR 3.1 MODIFIEDMODIFIEDA. BRUNGER, M. NILGESrefinement
Azarastructure solution
RefinementMethod: molecular dynamics / Software ordinal: 1
Details: AMBIGUOUS RESTRAINTS FOR ITERATIVE ASSIGNMENT METHOD (ARIA) DIRECT REFINEMENT AGAINST 1H-CHEMICAL SHIFTS
NMR ensembleConformer selection criteria: ENERGY, GEOMETRY, VIOLATIONS / Conformers calculated total number: 40 / Conformers submitted total number: 20

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