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- PDB-2mst: MUSASHI1 RBD2, NMR -

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Basic information

Entry
Database: PDB / ID: 2mst
TitleMUSASHI1 RBD2, NMR
ComponentsPROTEIN (MUSASHI1)
KeywordsRNA BINDING PROTEIN / RNA-BINDING DOMAIN
Function / homology
Function and homology information


: / poly(U) RNA binding / epithelial cell differentiation / response to hormone / central nervous system development / regulation of translation / single-stranded RNA binding / mRNA binding / identical protein binding / nucleus ...: / poly(U) RNA binding / epithelial cell differentiation / response to hormone / central nervous system development / regulation of translation / single-stranded RNA binding / mRNA binding / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
RNA-binding protein Musashi homologue, RNA recognition motif 2 / RRM (RNA recognition motif) domain / RNA recognition motif / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / RNA-binding domain superfamily / Nucleotide-binding alpha-beta plait domain superfamily / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
RNA-binding protein Musashi homolog 1
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodSOLUTION NMR / simulated annealing
AuthorsNagata, T. / Kanno, R. / Kurihara, Y. / Uesugi, S. / Imai, T. / Sakakibara, S. / Okano, H. / Katahira, M.
Citation
Journal: J.Mol.Biol. / Year: 1999
Title: Structure, backbone dynamics and interactions with RNA of the C-terminal RNA-binding domain of a mouse neural RNA-binding protein, Musashi1.
Authors: Nagata, T. / Kanno, R. / Kurihara, Y. / Uesugi, S. / Imai, T. / Sakakibara, S. / Okano, H. / Katahira, M.
#1: Journal: Gene / Year: 1997
Title: Structural Properties and RNA-Binding Activities of Two RNA Recognition Motifs of a Mouse Neural RNA-Binding Protein, Mouse-Musashi-1
Authors: Kurihara, Y. / Nagata, T. / Imai, T. / Hiwatashi, A. / Horiuchi, M. / Sakakibara, S. / Katahira, M. / Okano, H. / Uesugi, S.
History
DepositionMay 19, 1999Deposition site: BNL / Processing site: RCSB
Revision 1.0May 19, 2000Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 16, 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 1.4Dec 27, 2023Group: 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: PROTEIN (MUSASHI1)


Theoretical massNumber of molelcules
Total (without water)8,7301
Polymers8,7301
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)20 / 200LOWER ENERGIES
Representative

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Components

#1: Protein PROTEIN (MUSASHI1)


Mass: 8729.970 Da / Num. of mol.: 1 / Fragment: RNA-BINDING DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Description: PCR / Species (production host): Escherichia coli / Cell (production host): BL21(DE3) / Gene (production host): PET3A / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q61474

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121TOCSY
131DQF-COSY
1411H-15N 2D HSQC
15115N-EDITED NOESY-HSQC
16115N-EDITED TOCSY-HSQC
171HNHA

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Sample preparation

DetailsContents: 90% H2O/10% D2O
Sample conditionsIonic strength: 0 mM / pH: 6.0 / Pressure: 1 atm / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DRX600 / Manufacturer: Bruker / Model: DRX600 / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
X-PLOR3.8BRUNGERrefinement
X-PLOR3.1structure solution
X-PLOR3.8structure solution
RefinementMethod: simulated annealing / Software ordinal: 1
NMR ensembleConformer selection criteria: LOWER ENERGIES / Conformers calculated total number: 200 / Conformers submitted total number: 20

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