BMRB Entry 52303

Name: ZBP1 Tandem Zalpha Domains
Published: 2024-09-03

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52303

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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:

ZBP1 Tandem Zalpha Domains

Deposition date:

2024-02-02

Original release date:

2024-09-03

Authors:

Beck, Lily; Krall, Jeffrey; Nichols, Parker; Henen, Morkos; Vicens, Quentin; Vogeli, Beat

Citation:

Citation: Beck, Lily; Krall, Jeffrey; Nichols, Parker; Henen, Morkos; Vicens, Quentin; Vogeli, Beat. "Solution NMR backbone assignment of the N-terminal tandem Za1-Za2 domains of Z-DNA binding protein 1" Biomol. NMR Assign. ., .-. (2024).
PubMed: 39215796

Assembly members:

Assembly members:
entity_1, polymer, 213 residues, Formula weight is not available

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: pET-28a+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MASMTGGQQMGRGSMAQAPA DPGREGHLEQRILQVLTEAG SPVKLAQLVKECQAPKRELN QVLYRMKKELKVSLTSPATW CLGGTDPEGEGPAELALSSP AERPQQHAATIPETPGPQFS QQREEDIYRFLKDNGPQRAL VIAQALGMRTAKDVNRDLYR MKSRHLLDMDEQSKAWTIYR KLAAALEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	569
15N chemical shifts	197
1H chemical shifts	184

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ZBP1_Tandem	1

Entities:

Entity 1, ZBP1_Tandem 213 residues - Formula weight is not available

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

ALA

SER

MET

THR

GLY

GLN

MET

4

GLY

ARG

GLY

SER

MET

ALA

GLN

ALA

PRO

ALA

5

ASP

PRO

GLY

ARG

GLU

GLY

HIS

LEU

GLU

GLN

6

ARG

ILE

LEU

GLN

VAL

LEU

THR

GLU

ALA

GLY

7

SER

PRO

VAL

LYS

LEU

ALA

GLN

LEU

VAL

LYS

8

GLU

CYS

GLN

ALA

PRO

LYS

ARG

GLU

LEU

ASN

9

GLN

VAL

LEU

TYR

ARG

MET

LYS

GLU

LEU

10

LYS

VAL

SER

LEU

THR

SER

PRO

ALA

THR

TRP

11

CYS

LEU

GLY

THR

ASP

PRO

GLU

GLY

GLU

12

GLY

PRO

ALA

GLU

LEU

ALA

LEU

SER

PRO

13

ALA

GLU

ARG

PRO

GLN

HIS

ALA

THR

14

ILE

PRO

GLU

THR

PRO

GLY

PRO

GLN

PHE

SER

15

GLN

ARG

GLU

ASP

ILE

TYR

ARG

PHE

16

LEU

LYS

ASP

ASN

GLY

PRO

GLN

ARG

ALA

LEU

17

VAL

ILE

ALA

GLN

ALA

LEU

GLY

MET

ARG

THR

18

ALA

LYS

ASP

VAL

ASN

ARG

ASP

LEU

TYR

ARG

19

MET

LYS

SER

ARG

HIS

LEU

ASP

MET

ASP

20

GLU

GLN

SER

LYS

ALA

TRP

THR

ILE

TYR

ARG

21

LYS

LEU

ALA

LEU

GLU

HIS

22

HIS

Samples:

sample_1: ZBP1_Tandem, [U-100% 13C; U-100% 15N], 1.12 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.4; pressure: 1 atm; temperature: 308.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
2D (HCa)CON	sample_1	isotropic	sample_conditions_1
3D (H)N(CA)NNH	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - data analysis, processing

TOPSPIN v4.2.0 - collection, processing

CcpNMR v2.4.2 - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker AVANCE NEO 600 MHz

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