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- PDB-2rvj: NMR structure of Epithelial splicing regulatory protein 1 -

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Basic information

Entry
Database: PDB / ID: 2rvj
TitleNMR structure of Epithelial splicing regulatory protein 1
ComponentsEpithelial splicing regulatory protein 1
KeywordsTRANSCRIPTION
Function / homology
Function and homology information


regulation of inner ear auditory receptor cell fate specification / FGFR2 alternative splicing / regulation of RNA splicing / RNA splicing / mRNA processing / Signaling by BRAF and RAF1 fusions / nuclear body / ribonucleoprotein complex / mRNA binding / nucleoplasm / nucleus
Similarity search - Function
ESRP1, RNA recognition motif 1 / RRM (RNA recognition motif) domain / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / RNA-binding domain superfamily / Ribonuclease H superfamily / Ribonuclease H-like superfamily / Nucleotide-binding alpha-beta plait domain superfamily / Alpha-Beta Plaits ...ESRP1, RNA recognition motif 1 / RRM (RNA recognition motif) domain / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / RNA-binding domain superfamily / Ribonuclease H superfamily / Ribonuclease H-like superfamily / Nucleotide-binding alpha-beta plait domain superfamily / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Epithelial splicing regulatory protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
Model detailsfewest violations, model1
AuthorsYang, Y. / Allemand, F. / Guichou, J. / Labesse, G.
CitationJournal: To be Published
Title: NMR structure of Epithelial splicing regulatory protein 1
Authors: Yang, Y. / Allemand, F. / Guichou, J. / Labesse, G.
History
DepositionOct 23, 2015Deposition site: BMRB / Processing site: PDBJ
Revision 1.0Dec 23, 2015Provider: repository / Type: Initial release
Revision 1.1Jan 27, 2016Group: Database references
Revision 1.2Jun 14, 2023Group: Database references / Other
Category: database_2 / pdbx_database_status / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data / _struct_ref_seq_dif.details
Revision 1.3May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Epithelial splicing regulatory protein 1


Theoretical massNumber of molelcules
Total (without water)11,8351
Polymers11,8351
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)15 / 200structures with the lowest energy
RepresentativeModel #1fewest violations

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Components

#1: Protein Epithelial splicing regulatory protein 1 / RNA-binding motif protein 35A / RNA-binding protein 35A


Mass: 11834.680 Da / Num. of mol.: 1 / Fragment: UNP residues 438-539 / Mutation: V438M
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ESRP1, RBM35A / Production host: Escherichia coli (E. coli) / References: UniProt: Q6NXG1

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1213D 1H-13C NOESY aliphatic
1313D HNCA
1413D CBCA(CO)NH
1513D 1H-15N NOESY
1613D HNCO
1713D HBHA(CO)NH

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Sample preparation

DetailsContents: 0.6 mM [U-99% 13C; U-99% 15N] H2O-1, 90% H2O/10% D2O
Solvent system: 90% H2O/10% D2O
SampleConc.: 0.6 mM / Component: H2O-1 / Isotopic labeling: [U-99% 13C; U-99% 15N]
Sample conditionsIonic strength: 0.15 / pH: 5.4 / Pressure: ambient / Temperature: 305 K

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NMR measurement

NMR spectrometerType: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 700 MHz

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Processing

NMR software
NameVersionDeveloperClassification
CYANA2.1Guntert, Mumenthaler and Wuthrichgeometry optimization
CNSBrunger, Adams, Clore, Gros, Nilges and Readrefinement
CNS, _RECOORDscriptsrefinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: fewest violations
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 200 / Conformers submitted total number: 15 / Representative conformer: 1

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