BMRB Entry 50714

Name: Solution NMR backbone assignments of the N-terminal Za domain from Homo Sapiens ADAR1p150.
Published: 2021-03-21

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50714

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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:

Solution NMR backbone assignments of the N-terminal Za domain from Homo Sapiens ADAR1p150.

Deposition date:

2021-01-16

Original release date:

2021-03-21

Authors:

Nichols, Parker; Henen, Morks; Vicens, Quentin; Vogeli, Beat

Citation:

Citation: Nichols, Parker; Henen, Morks; Vicens, Quentin; Vogeli, Beat. "Solution NMR backbone assignments of the N-terminal Zalpha-linker-Zbeta segment from Homo sapiens ADAR1p150" Biomol. NMR Assign. 15, 273-279 (2021).
PubMed: 33742389

Assembly members:

Assembly members:
entity_1, polymer, 64 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: MEQRILKFLEELGEGKATTA HDLSGKLGTPKKEINRVLYS LAKKGKLQKEAGTPPLWKIA VSTQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	120
15N chemical shifts	124
1H chemical shifts	124

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Za	1

Entities:

Entity 1, Za 64 residues - Formula weight is not available

1

MET

GLU

GLN

ARG

ILE

LEU

LYS

PHE

LEU

GLU

2

GLU

LEU

GLY

GLU

GLY

LYS

ALA

THR

ALA

3

HIS

ASP

LEU

SER

GLY

LYS

LEU

GLY

THR

PRO

4

LYS

GLU

ILE

ASN

ARG

VAL

LEU

TYR

SER

5

LEU

ALA

LYS

GLY

LYS

LEU

GLN

LYS

GLU

6

ALA

GLY

THR

PRO

LEU

TRP

LYS

ILE

ALA

7

VAL

SER

THR

GLN

Samples:

sample_1: Za, [U-100% 13C; U-100% 15N], 2 mM; potassium phosphate 20 mM; NaCl 25 mM

sample_2: Za, [U-100% 13C; U-100% 15N], 2 mM; potassium phosphate 20 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 25 mM; pH: 6.4; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 100 mM; pH: 6.4; pressure: 1 atm; temperature: 308 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-15N HSQC	sample_2	isotropic	sample_conditions_2

Software:

NMRDraw v10.9 - processing

CcpNMR v2.4.2 - chemical shift assignment

NMR spectrometers:

Varian INOVA 900 MHz
Bruker Ultrashield 600 MHz

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