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- PDB-4uzx: High-resolution NMR structures of the domains of Saccharomyces ce... -

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Basic information

Entry
Database: PDB / ID: 4uzx
TitleHigh-resolution NMR structures of the domains of Saccharomyces cerevisiae Tho1
ComponentsPROTEIN THO1
KeywordsRNA BINDING PROTEIN / THO1
Function / homology
Function and homology information


poly(A)+ mRNA export from nucleus / protein-RNA complex assembly / transcription elongation by RNA polymerase II / double-stranded DNA binding / chromatin binding / RNA binding / nucleus
Similarity search - Function
THO1_MOS11, C-terminal domain / Tho1/MOS11 C-terminal domain / SAP domain superfamily / SAP domain / SAP motif profile. / Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation / SAP domain
Similarity search - Domain/homology
Biological speciesSACCHAROMYCES CEREVISIAE (brewer's yeast)
MethodSOLUTION NMR / CNS
AuthorsJacobsen, J.O.B. / Allen, M.D. / Freund, S.M.V. / Bycroft, M.
CitationJournal: Acta Crystallogr.,Sect.F / Year: 2016
Title: High-Resolution NMR Structures of the Domains of Saccharomyces Cerevisiae Tho1.
Authors: Jacobsen, J.O.B. / Allen, M.D. / Freund, S.M.V. / Bycroft, M.
History
DepositionSep 9, 2014Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 17, 2014Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2016Group: Atomic model / Other
Revision 1.2Jun 8, 2016Group: Database references
Revision 1.3Jun 29, 2016Group: Database references
Revision 1.4May 15, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_cs / _pdbx_database_status.status_code_mr

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PROTEIN THO1


Theoretical massNumber of molelcules
Total (without water)7,5011
Polymers7,5011
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 20NO VIOLATIONS
RepresentativeModel #1

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Components

#1: Protein PROTEIN THO1


Mass: 7501.494 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 119-183
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast)
Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P40040
Sequence detailsGLY-SER AT THE N-TERMINUS RESULTS FROM CLONING

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR detailsText: NONE

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Sample preparation

DetailsContents: 95% WATER/5% D2O
Sample conditionsIonic strength: 120 mM / pH: 6.5 / Pressure: 1.0 atm / Temperature: 293.0 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX5001
Bruker DRXBrukerDRX6002
Bruker DRXBrukerDRX8003

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Processing

NMR software
NameDeveloperClassification
CNSBRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- KUNSTLEVE, JIANG,KUSZEWSKI,NILGES,PANNU,READ, RICE,SIMONSON, WARRENrefinement
ANSIGstructure solution
CNSstructure solution
RefinementMethod: CNS / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE
NMR ensembleConformer selection criteria: NO VIOLATIONS / Conformers calculated total number: 20 / Conformers submitted total number: 20

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