BMRB Entry 27166

Name: 1H, 13C, and 15N Chemical Shift Assignments for LisH Domain of GID8
Published: 2017-08-04

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27166

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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:

1H, 13C, and 15N Chemical Shift Assignments for LisH Domain of GID8

Deposition date:

2017-07-03

Original release date:

2017-08-04

Authors:

Araujo, Talita; Almeida, Marcius

Citation:

Citation: Araujo, Talita; Almeida, Marcius. "1H, 13C and 15N chemical shift assignment of lissencephaly-1 homology (LisH) domain homodimer of human two-hybrid-associated protein 1 with RanBPM (Twa1)" Biomol. NMR Assign. 12, 99-102 (2018).
PubMed: 29067546

Assembly members:

Assembly members:
LisH-GID8, polymer, 59 residues, 6948.83 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: pET25b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
LisH-GID8: SYAEKPDEITKDEWMEKLNN LHVQRADMNRLIMNYLVTEG FKEAAEKFRMESGIEPSVD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	210
15N chemical shifts	54
1H chemical shifts	229

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	LisH, chain 1	1
2	LisH, chain 2	1

Entities:

Entity 1, LisH, chain 1 59 residues - 6948.83 Da.

This is the dimerization domain of the human protein GID8 (Glucose-induced degradation protein 8).

1

SER

TYR

ALA

GLU

LYS

PRO

ASP

GLU

ILE

THR

2

LYS

ASP

GLU

TRP

MET

GLU

LYS

LEU

ASN

3

LEU

HIS

VAL

GLN

ARG

ALA

ASP

MET

ASN

ARG

4

LEU

ILE

MET

ASN

TYR

LEU

VAL

THR

GLU

GLY

5

PHE

LYS

GLU

ALA

GLU

LYS

PHE

ARG

MET

6

GLU

SER

GLY

ILE

GLU

PRO

SER

VAL

ASP

Samples:

sample_1: LisH-GID8, [U-100% 13C; U-100% 15N], 0.7 mM; sodium phosphate 25 mM; sodium chloride 250 mM

sample_conditions_1: ionic strength: 0.25 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1

Software:

XEASY v1.9.1.5, Peter G ntert et al - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz
Bruker ASCEND 700 MHz
Bruker Avance 600 MHz

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