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- PDB-2kzs: DAXX helical bundle (DHB) domain -

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Basic information

Entry
Database: PDB / ID: 2kzs
TitleDAXX helical bundle (DHB) domain
ComponentsDeath-associated protein 6
KeywordsAPOPTOSIS / helical bundle / DHB domain / Fas death-domain associated protein / DAXX / Rassf1C interacting domain
Function / homology
Function and homology information


cellular response to diamide / Defective Inhibition of DNA Recombination at Telomere Due to DAXX Mutations / Defective Inhibition of DNA Recombination at Telomere Due to ATRX Mutations / SUMO-modified protein reader activity / neuron intrinsic apoptotic signaling pathway in response to oxidative stress / cellular response to sodium arsenite / transcription regulator inhibitor activity / nuclear androgen receptor binding / protein kinase activator activity / androgen receptor signaling pathway ...cellular response to diamide / Defective Inhibition of DNA Recombination at Telomere Due to DAXX Mutations / Defective Inhibition of DNA Recombination at Telomere Due to ATRX Mutations / SUMO-modified protein reader activity / neuron intrinsic apoptotic signaling pathway in response to oxidative stress / cellular response to sodium arsenite / transcription regulator inhibitor activity / nuclear androgen receptor binding / protein kinase activator activity / androgen receptor signaling pathway / chromosome, centromeric region / regulation of protein ubiquitination / extrinsic apoptotic signaling pathway via death domain receptors / positive regulation of protein kinase activity / cellular response to unfolded protein / JNK cascade / cellular response to copper ion / Inhibition of DNA recombination at telomere / heat shock protein binding / cellular response to cadmium ion / SUMOylation of transcription cofactors / molecular condensate scaffold activity / PML body / HCMV Early Events / transcription corepressor activity / nucleosome assembly / Regulation of TP53 Degradation / p53 binding / cellular response to heat / histone binding / regulation of gene expression / regulation of apoptotic process / RNA polymerase II-specific DNA-binding transcription factor binding / transcription coactivator activity / nuclear body / chromatin remodeling / positive regulation of protein phosphorylation / negative regulation of gene expression / negative regulation of DNA-templated transcription / ubiquitin protein ligase binding / regulation of DNA-templated transcription / nucleolus / protein kinase binding / enzyme binding / protein homodimerization activity / nucleoplasm / nucleus / cytosol
Similarity search - Function
Daxx helical bundle domain / Daxx, N-terminal Rassf1C-interacting domain / Daxx, N-terminal domain superfamily / Daxx, histone-binding domain / Daxx, histone-binding domain superfamily / Daxx N-terminal Rassf1C-interacting domain / Death domain-associated protein 6, histone binding domain / Helicase, Ruva Protein; domain 3 / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Death domain associated protein / Death domain-associated protein 6
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
Model detailslowest energy, model 2
AuthorsEscobar-Cabrera, E. / Lau, D.K.W. / Giovinazzi, S. / Ishov, A.M. / McIntosh, L.P.
CitationJournal: Structure / Year: 2010
Title: Structural Characterization of the DAXX N-Terminal Helical Bundle Domain and Its Complex with Rassf1C.
Authors: Escobar-Cabrera, E. / Lau, D.K. / Giovinazzi, S. / Ishov, A.M. / McIntosh, L.P.
History
DepositionJun 23, 2010Deposition site: BMRB / Processing site: RCSB
Revision 1.0Dec 15, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Feb 5, 2020Group: Database references / Other
Category: database_2 / pdbx_database_status / struct_ref_seq_dif
Item: _pdbx_database_status.status_code_cs / _struct_ref_seq_dif.details
Revision 1.3Jun 14, 2023Group: Database references / Other / Category: database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data
Revision 1.4May 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: Death-associated protein 6


Theoretical massNumber of molelcules
Total (without water)10,9511
Polymers10,9511
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)25 / 120structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein Death-associated protein 6 /


Mass: 10950.833 Da / Num. of mol.: 1 / Fragment: UNP residues 55 to 144
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Description: Cloned into pET28a from a human cDNA library, using NdeI and XhoI
Gene: DAXX, DADB-159G18.9-007, DAMC-227D19.15-007, DAQB-126H3.2-007, XXbac-BCX165D10.3-007, XXbac-BPG185D15.6-007
Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: Q4VX54, UniProt: Q9UER7*PLUS

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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 HN(CA)CB
1312D 1H-13C HSQC
1413D CBCA(CO)NH
1513D HBHA(CO)NH
1613D (H)CCH-TOCSY
1713D 1H-15N NOESY
1813D 1H-15N TOCSY
1913D 1H-13C NOESY
11013D H(CC)(CO)NH-TOCSY
11112D (HB)CB(CGCD)HD
11212D (HB)CBCGCDCE)HE
11312D HMBC
11422D 1H-13C HSQC
1151CT methyl-methyl-HSQC
1161CT amide-methyl-HSQC

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Sample preparation

Details
Solution-IDContentsSolvent system
11.2 mM [U-100% 13C; U-100% 15N] DAXX-1, 10 mM potassium phosphate-2, 100 mM KCl-3, 0.1 mM EDTA-4, 95% H2O/5% D2O95% H2O/5% D2O
20.8 mM [U-10% 13C] DAXX-5, 95% H2O/5% D2O95% H2O/5% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
1.2 mMDAXX-1[U-100% 13C; U-100% 15N]1
10 mMpotassium phosphate-21
100 mMKCl-31
0.1 mMEDTA-41
0.8 mMDAXX-5[U-10% 13C]2
Sample conditionsIonic strength: 0.16 / pH: 6.5 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian INOVAVarianINOVA6001
Varian UnityVarianUNITY5002

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Processing

NMR software
NameVersionDeveloperClassification
ARIA2.2Linge, O'Donoghue and Nilgesstructure solution
ARIA2.2Linge, O'Donoghue and Nilgessemi-automatic peak assignment
ARIA2.2Linge, O'Donoghue and Nilgesrefinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR constraintsNOE constraints total: 3585 / NOE intraresidue total count: 1153 / NOE long range total count: 761 / NOE medium range total count: 962 / NOE sequential total count: 709 / Protein chi angle constraints total count: 0 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 69 / Protein psi angle constraints total count: 69
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 120 / Conformers submitted total number: 25 / Maximum lower distance constraint violation: 0.02 Å / Maximum upper distance constraint violation: 0.28 Å

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