BMRB Entry 17018

Name: DAXX helical bundle (DHB) domain
Published: 2011-03-07

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PDB ID: 2kzs
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17018
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

DAXX helical bundle (DHB) domain

Deposition date:

2010-06-23

Original release date:

2011-03-07

Authors:

Escobar, 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).
PubMed: 21134643

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_NOEs
- heteronuclear_noe_list_1
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
heteronucl_T2_relaxation
- heteronuclear_T2_list_1
H_exch_rates
- H_exch_rate_list_1

Data type	Count
13C chemical shifts	428
15N chemical shifts	96
1H chemical shifts	697
heteronuclear NOE values	83
H exchange rates	25
T1 relaxation values	83
T2 relaxation values	83

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DAXX helical bundle	1

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

GLY

SER

HIS

MET

GLY

LYS

CYS

TYR

LYS

2

LEU

GLU

ASN

GLU

LYS

LEU

PHE

GLU

PHE

3

LEU

GLU

LEU

CYS

LYS

MET

GLN

THR

ALA

ASP

4

HIS

PRO

GLU

VAL

PRO

PHE

LEU

TYR

ASN

5

ARG

GLN

ARG

ALA

HIS

SER

LEU

PHE

LEU

6

ALA

SER

ALA

GLU

PHE

CYS

ASN

ILE

LEU

SER

7

ARG

VAL

LEU

SER

ARG

ALA

ARG

SER

ARG

PRO

8

ALA

LYS

LEU

TYR

VAL

TYR

ILE

ASN

GLU

LEU

9

CYS

THR

VAL

LEU

LYS

ALA

HIS

SER

ALA

LYS

10

LYS

LEU

ASN

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D H(CC)(CO)NH-TOCSY	sample_1	isotropic	sample_conditions_1
2D (HB)CB(CGCD)HD	sample_1	isotropic	sample_conditions_1
2D (HB)CBCGCDCE)HE	sample_1	isotropic	sample_conditions_1
2D HMBC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
CT methyl-methyl-HSQC	sample_1	isotropic	sample_conditions_1
CT amide-methyl-HSQC	sample_1	isotropic	sample_conditions_1
2D IPAP-HSQC	sample_2	anisotropic	sample_conditions_1
2D heteronuclear NOE	sample_1	isotropic	sample_conditions_1
2D T1	sample_1	isotropic	sample_conditions_1
2D T2	sample_1	isotropic	sample_conditions_1

Software:

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

SPARKY, Goddard -

NMR spectrometers:

Varian INOVA 600 MHz
Varian Unity 500 MHz

BMRB	17019
PDB	2KZS 2KZU
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
AlphaFold	Q9UER7