BMRB Entry 52311

Name: 1H, 13C and 15N backbone resonance assignments of the oncogenic protein NCYM
Published: 2025-02-06

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52311

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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 backbone resonance assignments of the oncogenic protein NCYM

Deposition date:

2024-02-07

Original release date:

2025-02-06

Authors:

Mouhand, Assia; Barthe, Philippe; Roumestand, Christian

Citation:

Citation: Mouhand, Assia; Nakatani, Kazuma; Kono, Fumiaki; Hippo, Yoshitaka; Matsuo, Tatsuhito; Barthe, Philippe; Peters, Judith; Suenaga, Yusuke; Tamada, Taro; Roumestand, Christian. "1H, 13C and 15N backbone and side-chain resonance assignments of the human oncogenic protein NCYM" Biomol. NMR Assign. 18, 65-70 (2024).
PubMed: 38526839

Assembly members:

Assembly members:
entity_1, polymer, 117 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: pGEX-6p-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPLGSPEFMQHPPCEPGNCL SLKEKKITEGSGGVCWGGET DASNPAPALTACCAAEREAN VEQGLAGRLLLCNYERRVVR RCKIAGRGRAPLGTRPLDVS SFKLKEEGRPPCLKINK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	309
15N chemical shifts	101
1H chemical shifts	637

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NCYM	1

Entities:

Entity 1, NCYM 117 residues - Formula weight is not available

Residues 1-8 represent a non-native tag

1

GLY

PRO

LEU

GLY

SER

PRO

GLU

PHE

MET

GLN

2

HIS

PRO

CYS

GLU

PRO

GLY

ASN

CYS

LEU

3

SER

LEU

LYS

GLU

LYS

ILE

THR

GLU

GLY

4

SER

GLY

VAL

CYS

TRP

GLY

GLU

THR

5

ASP

ALA

SER

ASN

PRO

ALA

PRO

ALA

LEU

THR

6

ALA

CYS

ALA

GLU

ARG

GLU

ALA

ASN

7

VAL

GLU

GLN

GLY

LEU

ALA

GLY

ARG

LEU

8

LEU

CYS

ASN

TYR

GLU

ARG

VAL

ARG

9

ARG

CYS

LYS

ILE

ALA

GLY

ARG

GLY

ARG

ALA

10

PRO

LEU

GLY

THR

ARG

PRO

LEU

ASP

VAL

SER

11

SER

PHE

LYS

LEU

LYS

GLU

GLY

ARG

PRO

12

PRO

CYS

LEU

LYS

ILE

ASN

LYS

Samples:

sample_1: NCYM, [U-100% 13C; U-100% 15N], 0.25 mM; potassium phosphate 50 mM; sodium chloride 50 mM; EDTA 0.1 mM; PMSF 0.1 mM; TCEP 2 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.1; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	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 HN(CA)CO	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

Software:

TOPSPIN v3.6 - collection, processing

CINDY v2.1 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 800 MHz

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