BMRB Entry 27653

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the N-terminal Domain of ING5
Published: 2019-06-18

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27653

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for the N-terminal Domain of ING5

Deposition date:

2018-10-17

Original release date:

2019-06-18

Authors:

Blanco, Francisco J; Ibanez de Opakua, Alain; Ormaza, Georgina; Rodriguez, Jhon Alexander

Citation:

Citation: Ormaza, Georgina; Rodriguez, Jhon; Ibanez de Opakua, Alain; Merino, Nekane; Villate, Maider; Gorrono, Irantzu; Rabano, Miriam; Palmero, Ignacio; Vilaseca, Marta; Kypta, Robert; Vivanco, Maria; Rojas, Adriana; Blanco, Francisco. "The Tumor Suppressor ING5 Is a Dimeric, Bivalent Recognition Molecule of the Histone H3K4me3 Mark." J. Mol. Biol. 431, 2298-2319 (2019).
PubMed: 31026448

Assembly members:

Assembly members:
ING5_Nterminal, polymer, 107 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: pet11d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ING5_Nterminal: GAMATAMYLEHYLDSIENLP CELQRNFQLMRELDQRTEDK KAEIDILAAEYISTVKTLSP DQRVERLQKIQNAYSKCKEY SDDKVQLAMQTYEMVDKHIR RLDADLA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	209
15N chemical shifts	94
1H chemical shifts	137

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ING5 Nterminal, subunit 1	1
2	ING5 Nterminal, subunit 2	1

Entities:

Entity 1, ING5 Nterminal, subunit 1 107 residues - Formula weight is not available

1

GLY

ALA

MET

ALA

THR

ALA

MET

TYR

LEU

GLU

2

HIS

TYR

LEU

ASP

SER

ILE

GLU

ASN

LEU

PRO

3

CYS

GLU

LEU

GLN

ARG

ASN

PHE

GLN

LEU

MET

4

ARG

GLU

LEU

ASP

GLN

ARG

THR

GLU

ASP

LYS

5

LYS

ALA

GLU

ILE

ASP

ILE

LEU

ALA

GLU

6

TYR

ILE

SER

THR

VAL

LYS

THR

LEU

SER

PRO

7

ASP

GLN

ARG

VAL

GLU

ARG

LEU

GLN

LYS

ILE

8

GLN

ASN

ALA

TYR

SER

LYS

CYS

LYS

GLU

TYR

9

SER

ASP

LYS

VAL

GLN

LEU

ALA

MET

GLN

10

THR

TYR

GLU

MET

VAL

ASP

LYS

HIS

ILE

ARG

11

ARG

LEU

ASP

ALA

ASP

LEU

ALA

Samples:

sample_1: ING5 Nterminal, [U-99% 13C; U-99% 15N], 364 mM; MOPS 50 mM; DTT 1 mM; sodium azide 0.01 % w/v; DSS 25 uM; D2O, [U-100% 2H], 5 % v/v; Protease inhibitors 1 tablet/100mL

sample_conditions_1: pH: 7.25; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C 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 HN(CO)CA	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 HN(CA)HA	sample_1	isotropic	sample_conditions_1
3D HN(COCA)HA	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

MARS, Zweckstetter - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

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