BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17018

Title: DAXX helical bundle (DHB) domain   PubMed: 21134643

Authors: Escobar, Eric; McIntosh, Lawrence

Citation: Escobar-Cabrera, Eric; Lau, Desmond; Giovinazzi, Serena; Alexander, Ishov; McIntosh, Lawrence. "Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C"  Structure 18, 1642-1653 (2010).

Assembly members:
DAXX, polymer, 94 residues, 10950.916 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
DAXX: GSHMGKKCYKLENEKLFEEF LELCKMQTADHPEVVPFLYN RQQRAHSLFLASAEFCNILS RVLSRARSRPAKLYVYINEL CTVLKAHSAKKKLN

Data sets:
Data typeCount
13C chemical shifts428
15N chemical shifts96
1H chemical shifts697
heteronuclear NOE values83
H exchange rates25
T1 relaxation values83
T2 relaxation values83

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1DAXX helical bundle1

Entities:

Entity 1, DAXX helical bundle 94 residues - 10950.916 Da.

Residues 51-54 represent are non-native, and resulted from removing a His-tag with thrombin from a pET28a construct.

1   GLYSERHISMETGLYLYSLYSCYSTYRLYS
2   LEUGLUASNGLULYSLEUPHEGLUGLUPHE
3   LEUGLULEUCYSLYSMETGLNTHRALAASP
4   HISPROGLUVALVALPROPHELEUTYRASN
5   ARGGLNGLNARGALAHISSERLEUPHELEU
6   ALASERALAGLUPHECYSASNILELEUSER
7   ARGVALLEUSERARGALAARGSERARGPRO
8   ALALYSLEUTYRVALTYRILEASNGLULEU
9   CYSTHRVALLEULYSALAHISSERALALYS
10   LYSLYSLEUASN

Samples:

sample_1: DAXX, [U-100% 13C; U-100% 15N], 1.2 mM; potassium phosphate 10 mM; KCl 100 mM; EDTA 0.1 mM; H2O 95%; D2O 5%

sample_2: DAXX, [U-10% 13C], 0.8 mM; potassium phosphate 10 mM; KCl 100 mM; EDTA 0.1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.16 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D H(CC)(CO)NH-TOCSYsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D (HB)CBCGCDCE)HEsample_1isotropicsample_conditions_1
2D HMBCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
CT methyl-methyl-HSQCsample_1isotropicsample_conditions_1
CT amide-methyl-HSQCsample_1isotropicsample_conditions_1
2D IPAP-HSQCsample_2anisotropicsample_conditions_1
2D heteronuclear NOEsample_1isotropicsample_conditions_1
2D T1sample_1isotropicsample_conditions_1
2D T2sample_1isotropicsample_conditions_1

Software:

ARIA v2.2, Linge, O, . - semi-automatic peak assignment, structure solution

SPARKY, Goddard -

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian Unity 500 MHz

Related Database Links:

BMRB 17019
PDB
DBJ BAA34295 BAD92730 BAF84876 BAG35867 BAG64733
EMBL CAB09986 CAB09989 CAG33366
GB AAB66585 AAB92671 AAC39853 AAC72843 AAI09074
REF NP_001135441 NP_001135442 NP_001241646 NP_001341 XP_001170728
SP Q9UER7