BMRB Entry 50942

Name: NMR backbone resonance assignment of the pro-apoptotic Bak in its apo state
Published: 2021-06-15

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50942

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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:

NMR backbone resonance assignment of the pro-apoptotic Bak in its apo state

Deposition date:

2021-05-14

Original release date:

2021-06-15

Authors:

Sperl, Laura; Hagn, Franz

Citation:

Citation: Sperl, Laura; Ruehrnoessl, Florian; Schiller, Anita; Haslbeck, Martin; Hagn, Franz. "High-resolution analysis of the conformational transition of pro-apoptotic Bak at the lipid membrane" EMBO J. 40, e107159-e107159 (2021).
PubMed: 34523144

Assembly members:

Assembly members:
entity_1, polymer, 214 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: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MEASASGQGPGPPRQECGEP ALPSASEEQVAQDTEEVFRS YVFYRHQQEQEAEGVAAPAD PEMVTLPLQPSSTMGQVGRQ LAIIGDDINRRYDSEFQTML QHLQPTAENAYEYFTKIATS LFESGINWGRVVALLGFGYR LALHVYQHGLTGFLGQVTRF VVDFMLHHCIARWIAQRGGW VAALNLGNGPILNVLVVLGV VLLGQFVVRRFFKS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	398
15N chemical shifts	139
1H chemical shifts	139

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Bak	1

Entities:

Entity 1, Bak 214 residues - Formula weight is not available

1

MET

GLU

ALA

SER

ALA

SER

GLY

GLN

GLY

PRO

2

GLY

PRO

ARG

GLN

GLU

CYS

GLY

GLU

PRO

3

ALA

LEU

PRO

SER

ALA

SER

GLU

GLN

VAL

4

ALA

GLN

ASP

THR

GLU

VAL

PHE

ARG

SER

5

TYR

VAL

PHE

TYR

ARG

HIS

GLN

GLU

GLN

6

GLU

ALA

GLU

GLY

VAL

ALA

PRO

ALA

ASP

7

PRO

GLU

MET

VAL

THR

LEU

PRO

LEU

GLN

PRO

8

SER

THR

MET

GLY

GLN

VAL

GLY

ARG

GLN

9

LEU

ALA

ILE

GLY

ASP

ILE

ASN

ARG

10

ARG

TYR

ASP

SER

GLU

PHE

GLN

THR

MET

LEU

11

GLN

HIS

LEU

GLN

PRO

THR

ALA

GLU

ASN

ALA

12

TYR

GLU

TYR

PHE

THR

LYS

ILE

ALA

THR

SER

13

LEU

PHE

GLU

SER

GLY

ILE

ASN

TRP

GLY

ARG

14

VAL

ALA

LEU

GLY

PHE

GLY

TYR

ARG

15

LEU

ALA

LEU

HIS

VAL

TYR

GLN

HIS

GLY

LEU

16

THR

GLY

PHE

LEU

GLY

GLN

VAL

THR

ARG

PHE

17

VAL

ASP

PHE

MET

LEU

HIS

CYS

ILE

18

ALA

ARG

TRP

ILE

ALA

GLN

ARG

GLY

TRP

19

VAL

ALA

LEU

ASN

LEU

GLY

ASN

GLY

PRO

20

ILE

LEU

ASN

VAL

LEU

VAL

LEU

GLY

VAL

21

VAL

LEU

GLY

GLN

PHE

VAL

ARG

22

PHE

LYS

SER

Samples:

sample_1: Bak, [U-100% 13C; U-100% 15N], 200 uM; sodium phosphate 20 mM; EDTA 0.5 mM; DTT 2 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 303 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 15N-separated NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection, processing

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 950 MHz

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