BMRB Entry 17019

Title:
DAXX helical bundle (DHB) domain / Rassf1C complex   PubMed: 21134643
Deposition date:
2010-06-25
Original release date:
2011-03-07
Authors:
Escobar-Cabrera, Eric; McIntosh, Lawrence
Citation:

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:

Assembly members:
DAXX, polymer, 94 residues, 10950.916 Da.
Rassf1C, polymer, 18 residues, 2149.186 Da.

Natural source:

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   Vector: pET28a

Experimental source:

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   Vector: pET28a

Data sets:
Data typeCount
13C chemical shifts387
15N chemical shifts115
1H chemical shifts790

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DAXX1
2Rassf1C2

Entities:

Entity 1, DAXX 94 residues - 10950.916 Da.

residues 51-54 are residual from removing the 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

Entity 2, Rassf1C 18 residues - 2149.186 Da.

residue 22 is residual from removing the GST with thrombin from a PGEX construct Residue 39 is non-native, introduced to quantify the peptide.

1   GLYSERGLNGLUASPSERASPSERGLULEU
2   GLUGLNTYRPHETHRALAARGTRP

Samples:

Dr: DAXX, [U-100% 13C; U-100% 15N], 1.1 mM; Rassf1C 1.65 mM; H2O 95%; D2O 5%

Rd: DAXX 1.8 mM; Rassf1C, [U-100% 13C; U-100% 15N], 1.2 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCDrisotropicsample_conditions_1
2D 1H-15N HSQCRdisotropicsample_conditions_1
3D CBCA(CO)NHRdisotropicsample_conditions_1
3D HNCACBRdisotropicsample_conditions_1
3D CBCA(CO)NHDrisotropicsample_conditions_1
3D HCCH-TOCSYDrisotropicsample_conditions_1
2D 1H-13C HSQCDrisotropicsample_conditions_1
(H)CC(CO)NH-TOCSYDrisotropicsample_conditions_1
HCC(CO)NH-TOCSYDrisotropicsample_conditions_1
(HB)CB(CGCD)HDDrisotropicsample_conditions_1
(HB)CB(CGCDCE)HEDrisotropicsample_conditions_1
3D 1H-15N NOESYDrisotropicsample_conditions_1
3D 1H-13C NOESYDrisotropicsample_conditions_1
13C/15N isotope-filtered NOESY-HSQCDrisotropicsample_conditions_1
13C/15N isotope-filtered NOESY-HSQCRdisotropicsample_conditions_1
3D 1H-15N NOESYRdisotropicsample_conditions_1
3D 1H-13C NOESYRdisotropicsample_conditions_1
2D 1H-13C HSQCRdisotropicsample_conditions_1
(H)CC(CO)NH-TOCSYRdisotropicsample_conditions_1
HCC(CO)NH-TOCSYRdisotropicsample_conditions_1
(HB)CB(CGCD)HDRdisotropicsample_conditions_1
(HB)CB(CGCD)HD-TOCSYRdisotropicsample_conditions_1
3D 1H-15N TOCSYRdisotropicsample_conditions_1

Software:

ARIA v2.2, Linge, O'Donoghue and Nilges - refinement, semi automatic peak assignments, structure solution

NMR spectrometers:

  • Varian Unity 600 MHz

Related Database Links:

BMRB 17018
PDB
DBJ BAA34295 BAD92730 BAF84876 BAG35867 BAG64733 BAF85327
EMBL CAB09986 CAB09989 CAG33366
GB AAB66585 AAB92671 AAC39853 AAC72843 AAI09074 AAC16001 AAC70910 AAD30061 AAD44175 AAH02173
REF NP_001135441 NP_001135442 NP_001241646 NP_001341 XP_001170728 NP_001007755 NP_001068910 NP_062687 NP_733831 XP_001100583
SP Q9UER7
TPG DAA16909
AlphaFold Q9UER7

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts