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- PDB-2hfh: THE NMR STRUCTURES OF A WINGED HELIX PROTEIN: GENESIS, 20 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 2hfh
TitleTHE NMR STRUCTURES OF A WINGED HELIX PROTEIN: GENESIS, 20 STRUCTURES
ComponentsGENESIS
KeywordsHNF-3 HOMOLOGUES / WINGED HELIX PROTEIN
Function / homology
Function and homology information


trophectodermal cell differentiation / embryonic placenta development / cellular response to leukemia inhibitory factor / RNA polymerase II transcription regulatory region sequence-specific DNA binding / DNA-binding transcription repressor activity, RNA polymerase II-specific / sequence-specific double-stranded DNA binding / double-stranded DNA binding / in utero embryonic development / transcription cis-regulatory region binding / DNA-binding transcription factor activity ...trophectodermal cell differentiation / embryonic placenta development / cellular response to leukemia inhibitory factor / RNA polymerase II transcription regulatory region sequence-specific DNA binding / DNA-binding transcription repressor activity, RNA polymerase II-specific / sequence-specific double-stranded DNA binding / double-stranded DNA binding / in utero embryonic development / transcription cis-regulatory region binding / DNA-binding transcription factor activity / chromatin / regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / DNA binding / nucleus
Similarity search - Function
: / Fork head domain conserved site1 / Fork head domain signature 1. / Fork head domain / Forkhead domain / Fork head domain profile. / FORKHEAD / Fork head domain conserved site 2 / Fork head domain signature 2. / Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain ...: / Fork head domain conserved site1 / Fork head domain signature 1. / Fork head domain / Forkhead domain / Fork head domain profile. / FORKHEAD / Fork head domain conserved site 2 / Fork head domain signature 2. / Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain / Arc Repressor Mutant, subunit A / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Forkhead box protein D3
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodSOLUTION NMR / DIANA
AuthorsMarsden, I. / Jin, C. / Liao, X.
Citation
Journal: J.Mol.Biol. / Year: 1998
Title: Structural changes in the region directly adjacent to the DNA-binding helix highlight a possible mechanism to explain the observed changes in the sequence-specific binding of winged helix proteins.
Authors: Marsden, I. / Jin, C. / Liao, X.
#1: Journal: Biochemistry / Year: 1997
Title: Evidence that the DNA Binding Specificity of Winged Helix Proteins is Mediated by a Structural Change in the Amino Acid Sequence Adjacent to the Principal DNA Binding Helix
Authors: Marsden, I. / Chen, Y. / Jin, C. / Liao, X.
History
DepositionJan 27, 1998Processing site: BNL
Revision 1.0Jun 17, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 9, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: GENESIS


Theoretical massNumber of molelcules
Total (without water)13,0491
Polymers13,0491
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 / 100LOWEST TARGET FUNCTION
Representative

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Components

#1: Protein GENESIS / HFH-2


Mass: 13049.021 Da / Num. of mol.: 1 / Fragment: DNA-BINDING DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Description: FIRST PUBLISHED IN PNAS 90, 3948-3952 / Cell line: 293 / Cellular location: NUCLEUSCell nucleus / Gene: HFH-2, GENESIS / Organ: LIVER, LUNG, HEART / Plasmid: PET21 / Gene (production host): T7 / Organelle (production host): INCLUSION BODIES / Production host: Escherichia coli (E. coli) / Strain (production host): HMS-174 / References: UniProt: Q63245

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESYHSQC
121HNCA
131HN(CA)CB
141CBCA(CO)HN
151HBHA(CO)HN
161HCCHTOCSY
171NOESY

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Sample preparation

Sample conditionspH: 6.5 / Temperature: 290 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DMX500BrukerDMX5005001
Varian UNITY PLUS 500VarianUNITY PLUS 5005002

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Processing

NMR software
NameDeveloperClassification
DIANAGUNTERT,WUTHRICHrefinement
TRIADstructure solution
RefinementMethod: DIANA / Software ordinal: 1
NMR ensembleConformer selection criteria: LOWEST TARGET FUNCTION / Conformers calculated total number: 100 / Conformers submitted total number: 20

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