BMRB Entry 52601

Name: Backbone NMR assignments of the human BACH1 BTB domain
Published: 2024-12-02

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52601

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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:

Backbone NMR assignments of the human BACH1 BTB domain

Deposition date:

2024-09-10

Original release date:

2024-12-02

Authors:

Goretzki, Benedikt; Cesar, Fernandez

Citation:

Citation: Goretzki, Benedikt; Khoshouei, Maryam; Schroder, Martin; Penner, Patrick; Egger, Luca; Stephan, Christine; Argoti, Dayana; Dierlamm, Nele; Rada, Jimena Maria; Kapps, Sandra; Muller, Catrin Swantje; Thiel, Zacharias; Mutlu, Merve; Tschopp, Claude; Furkert, David; Freuler, Felix; Haenni, Simon; Tenaillon, Laurent; Knapp, Britta; Hinniger, Alexandra; Hoppe, Philipp; Schmidt, Enrico; Gutmann, Sascha; Iurlaro, Mario; Ryzhakov, Grigory; Fernandez, Cesar. "Dual BACH1 regulation by complementary SCF-type E3 ligases" Cell 187, 7585-7602 (2024).
PubMed: 39657677

Assembly members:

Assembly members:
entity_1, polymer, 124 residues, 14042.06 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: pJ201

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SMSVFAYESSVHSTNVLLSL NDQRKKDVLCDVTIFVEGQR FRAHRSVLAACSSYFHSRIV GQADGELNITLPEEVTVKGF EPLIQFAYTAKLILSKENVD EVCKCVEFLSVHNIEESCFQ FLKF

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	199
15N chemical shifts	117
1H chemical shifts	117

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BACH1 BTB domain	1

Entities:

Entity 1, BACH1 BTB domain 124 residues - 14042.06 Da.

The first two residues (SM) are non-native residues which stem from a protease cleavage site.

1

SER

MET

SER

VAL

PHE

ALA

TYR

GLU

SER

2

VAL

HIS

SER

THR

ASN

VAL

LEU

SER

LEU

3

ASN

ASP

GLN

ARG

LYS

ASP

VAL

LEU

CYS

4

ASP

VAL

THR

ILE

PHE

VAL

GLU

GLY

GLN

ARG

5

PHE

ARG

ALA

HIS

ARG

SER

VAL

LEU

ALA

6

CYS

SER

TYR

PHE

HIS

SER

ARG

ILE

VAL

7

GLY

GLN

ALA

ASP

GLY

GLU

LEU

ASN

ILE

THR

8

LEU

PRO

GLU

VAL

THR

VAL

LYS

GLY

PHE

9

GLU

PRO

LEU

ILE

GLN

PHE

ALA

TYR

THR

ALA

10

LYS

LEU

ILE

LEU

SER

LYS

GLU

ASN

VAL

ASP

11

GLU

VAL

CYS

LYS

CYS

VAL

GLU

PHE

LEU

SER

12

VAL

HIS

ASN

ILE

GLU

SER

CYS

PHE

GLN

13

PHE

LEU

LYS

PHE

Samples:

sample_1: BACH1 BTB domain, [U-13C; U-15N; U-2H], 500 uM; D2O 5%; DSS 150 uM; sodium chloride 150 mM; HEPES, [U-2H], 25 mM; TCEP, [U-2H], 1 mM; glycerol, [U-2H], 5%

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 296 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v4 - collection, data analysis, processing

CcpNMR v3 - chemical shift assignment, data analysis

NMR spectrometers:

Bruker AVANCE III 800 MHz