BMRB Entry 19045

Name: The NMR structure of the BID-BAK complex
Published: 2013-04-15

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PDB ID: 2m5b
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19045
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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:

The NMR structure of the BID-BAK complex

Deposition date:

2013-02-19

Original release date:

2013-04-15

Authors:

Grace, Christy; Kriwacki, Richard; Green, Douglas

Citation:

Citation: Moldoveanu, Tudor; Grace, Christy; Llambi, Fabien; Nourse, Amanda; Fitzgerald, Patrick; Gehring, Kalle; Kriwacki, Richard; Green, Douglas. "BID-induced structural changes in BAK promote apoptosis." Nat. Struct. Mol. Biol. 20, 589-597 (2013).
PubMed: 23604079

Assembly members:

Assembly members:
human_cBAK, polymer, 169 residues, 18950.404 Da.
human_BID_BH3_SAHB, polymer, 23 residues, 2278.613 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: Amp resistant pET variant

Entity Sequences (FASTA):

Entity Sequences (FASTA):
human_cBAK: ALPSASEEQVAQDTEEVFRS YVFYRHQQEQEAEGVAAPAD PEMVTLPLQPSSTMGQVGRQ LAIIGDDINRRYDSEFQTML QHLQPTAENAYEYFTKIATS LFESGINWGRVVALLGFGYR LALHVYQHGLTGFLGQVTRF VVDFMLHHCIARWIAQRGGW VAALNLGNG
human_BID_BH3_SAHB: EDIIRNIARHLAXVGDXXDR SIX

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	556
15N chemical shifts	176
1H chemical shifts	1363

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	human_cBAK	1
2	human_BID_BH3_SAHB	2

Entities:

Entity 1, human_cBAK 169 residues - 18950.404 Da.

1

ALA

LEU

PRO

SER

ALA

SER

GLU

GLN

VAL

2

ALA

GLN

ASP

THR

GLU

VAL

PHE

ARG

SER

3

TYR

VAL

PHE

TYR

ARG

HIS

GLN

GLU

GLN

4

GLU

ALA

GLU

GLY

VAL

ALA

PRO

ALA

ASP

5

PRO

GLU

MET

VAL

THR

LEU

PRO

LEU

GLN

PRO

6

SER

THR

MET

GLY

GLN

VAL

GLY

ARG

GLN

7

LEU

ALA

ILE

GLY

ASP

ILE

ASN

ARG

8

ARG

TYR

ASP

SER

GLU

PHE

GLN

THR

MET

LEU

9

GLN

HIS

LEU

GLN

PRO

THR

ALA

GLU

ASN

ALA

10

TYR

GLU

TYR

PHE

THR

LYS

ILE

ALA

THR

SER

11

LEU

PHE

GLU

SER

GLY

ILE

ASN

TRP

GLY

ARG

12

VAL

ALA

LEU

GLY

PHE

GLY

TYR

ARG

13

LEU

ALA

LEU

HIS

VAL

TYR

GLN

HIS

GLY

LEU

14

THR

GLY

PHE

LEU

GLY

GLN

VAL

THR

ARG

PHE

15

VAL

ASP

PHE

MET

LEU

HIS

CYS

ILE

16

ALA

ARG

TRP

ILE

ALA

GLN

ARG

GLY

TRP

17

VAL

ALA

LEU

ASN

LEU

GLY

ASN

GLY

Entity 2, human_BID_BH3_SAHB 23 residues - 2278.613 Da.

1

GLU

ASP

ILE

ARG

ASN

ILE

ALA

ARG

HIS

2

LEU

ALA

MK8

VAL

GLY

ASP

MK8

NLE

ASP

ARG

3

SER

ILE

NH2

Samples:

SAHB-BAK: human cBAK, [U-98% 13C; U-98% 15N], 0.5 mM; human BID BH3 SAHB 0.5 mM; Phosphate buffer 20 mM

sample_conditions_1: ionic strength: 0.02 M; pH: 6.8; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	SAHB-BAK	isotropic	sample_conditions_1
2D 1H-13C HSQC	SAHB-BAK	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	SAHB-BAK	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	SAHB-BAK	isotropic	sample_conditions_1
2D 1H-1H TOCSY	SAHB-BAK	isotropic	sample_conditions_1
2D 1H-1H COSY	SAHB-BAK	isotropic	sample_conditions_1
3D CBCA(CO)NH	SAHB-BAK	isotropic	sample_conditions_1
3D HNCA	SAHB-BAK	isotropic	sample_conditions_1
3D HNCACB	SAHB-BAK	isotropic	sample_conditions_1
3D HBHA(CBCACO)NH	SAHB-BAK	isotropic	sample_conditions_1
3D 1H HCCH-TOCSY	SAHB-BAK	isotropic	sample_conditions_1
3D 13C-detected HCC-TOCSY	SAHB-BAK	isotropic	sample_conditions_1
2D 1H-15N TROSY	SAHB-BAK	isotropic	sample_conditions_1
3D 1H-15N NOESY	SAHB-BAK	isotropic	sample_conditions_1
3D 1H-15N TOCSY	SAHB-BAK	isotropic	sample_conditions_1
3D 1H-13C NOESY	SAHB-BAK	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	SAHB-BAK	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	SAHB-BAK	isotropic	sample_conditions_1
2D 13C-1H TROSY	SAHB-BAK	isotropic	sample_conditions_1
3D 13C/15N half-filtered 15N-edited NOESY	SAHB-BAK	isotropic	sample_conditions_1
3D 13C/15N half-filtered 13C-edited NOESY	SAHB-BAK	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin, Guntert, Mumenthaler and Wuthrich, Keller and Wuthrich - chemical shift assignment, processing, structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

GB	AAA74466 AAA74466 AAA93066 AAH04431 AAO74828 AAX32376 CAG30275
PDB	2IMS 2IMT 2JCN 2M5B 2YV6 4U2U 2M5B
DBJ	BAA13606 BAF84782 BAG52419 BAG57025 BAG64474
EMBL	CAA58997 CAG33700 CAI46254
PRF	2110382A 2110383A 2110384A
REF	NP_001179 NP_001253660 XP_003808607 XP_003897507 XP_003897509
SP	Q16611
AlphaFold	Q16611