BMRB Entry 50803

Name: Chemical shift assignment of NDRG1-C, the C-terminal domain of NDRG1
Published: 2022-10-13

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50803

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Chemical shift assignment of NDRG1-C, the C-terminal domain of NDRG1 PubMed: 36139110

Deposition date: 2021-03-07 Original release date: 2022-10-13

Authors: Ciurli, Stefano; Zambelli, Barbara

Citation: Beniamino, Ylenia; Cenni, Vittoria; Piccioli, Mario; Ciurli, Stefano; Zambelli, Barbara. "The Ni(II)-Binding Activity of the Intrinsically Disordered Region of Human NDRG1, a Protein Involved in Cancer Development" Biomolecules 12, 1272-1272 (2022).

Assembly members:
entity_1, polymer, 85 residues, 8826.57 Da.

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: pETZZ_1a

Entity Sequences (FASTA):
entity_1: GHMGYMPSASMTRLMRSRTA SGSSVTSLDGTRSRSHTSEG TRSRSHTSEGTRSRSHTSEG AHLDITPNSGAAGNSAGPKS MEVSC

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	322
15N chemical shifts	81
1H chemical shifts	481

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NDRG1-C	1

Entities:

Entity 1, NDRG1-C 85 residues - 8826.57 Da.

1

GLY

HIS

MET

GLY

TYR

MET

PRO

SER

ALA

SER

2

MET

THR

ARG

LEU

MET

ARG

SER

ARG

THR

ALA

3

SER

GLY

SER

VAL

THR

SER

LEU

ASP

GLY

4

THR

ARG

SER

ARG

SER

HIS

THR

SER

GLU

GLY

5

THR

ARG

SER

ARG

SER

HIS

THR

SER

GLU

GLY

6

THR

ARG

SER

ARG

SER

HIS

THR

SER

GLU

GLY

7

ALA

HIS

LEU

ASP

ILE

THR

PRO

ASN

SER

GLY

8

ALA

GLY

ASN

SER

ALA

GLY

PRO

LYS

SER

9

MET

GLU

VAL

SER

CYS

Samples:

sample_1: NDRG1-C, [U-100% 13C; U-100% 15N], 0.9 ± 0.05 mM; HEPES 20 mM; NaCl 150 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 0.15 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 HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHANH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDHD	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDCEHE	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v4.0.3 - collection

NMRPipe v10.9 - processing

NMRFAM-SPARKY v3.19 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 1200 MHz

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