BMRB Entry 18792

Name: Solution structure of BCL-xL determined with selective isotope labelling of I,L,V sidechains
Published: 2013-01-22

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PDB ID: 2m03
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18792
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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:

Solution structure of BCL-xL determined with selective isotope labelling of I,L,V sidechains

Deposition date:

2012-10-19

Original release date:

2013-01-22

Authors:

Viacava Follis, Ariele; Royappa, Grace; Kriwacki, Richard

Citation:

Citation: Follis, Ariele Viacava; Chipuk, Jerry; Fisher, John; Yun, Mi-Kyung; Grace, Christy; Nourse, Amanda; Baran, Katherine; Ou, Li; Min, Lie; White, Stephen; Green, Douglas; Kriwacki, Richard. "PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis." Nat. Chem. Biol. 9, 163-168 (2013).
PubMed: 23340338

Assembly members:

Assembly members:
BCL-xL_apo, polymer, 181 residues, 20252.496 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: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BCL-xL_apo: MSMAMSQSNRELVVDFLSYK LSQKGYSWSQFSDVEENRTE APEGTESEAVKQALREAGDE FELRYRRAFSDLTSQLHITP GTAYQSFEQVVNELFRDGVN WGRIVAFFSFGGALCVESVD KEMQVLVSRIAAWMATYLND HLEPWIQENGGWDTFVELYG NNAAAESRKGQERLEHHHHH H

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	536
15N chemical shifts	171
1H chemical shifts	343

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BCL-xL_apo	1

Entities:

Entity 1, BCL-xL_apo 181 residues - 20252.496 Da.

Wild-type Human protein with truncation of 22 C terminal residues and disordered loop between alpha helices 1 and 2

1

MET

SER

MET

ALA

MET

SER

GLN

SER

ASN

ARG

2

GLU

LEU

VAL

ASP

PHE

LEU

SER

TYR

LYS

3

LEU

SER

GLN

LYS

GLY

TYR

SER

TRP

SER

GLN

4

PHE

SER

ASP

VAL

GLU

ASN

ARG

THR

GLU

5

ALA

PRO

GLU

GLY

THR

GLU

SER

GLU

ALA

VAL

6

LYS

GLN

ALA

LEU

ARG

GLU

ALA

GLY

ASP

GLU

7

PHE

GLU

LEU

ARG

TYR

ARG

ALA

PHE

SER

8

ASP

LEU

THR

SER

GLN

LEU

HIS

ILE

THR

PRO

9

GLY

THR

ALA

TYR

GLN

SER

PHE

GLU

GLN

VAL

10

VAL

ASN

GLU

LEU

PHE

ARG

ASP

GLY

VAL

ASN

11

TRP

GLY

ARG

ILE

VAL

ALA

PHE

SER

PHE

12

GLY

ALA

LEU

CYS

VAL

GLU

SER

VAL

ASP

13

LYS

GLU

MET

GLN

VAL

LEU

VAL

SER

ARG

ILE

14

ALA

TRP

MET

ALA

THR

TYR

LEU

ASN

ASP

15

HIS

LEU

GLU

PRO

TRP

ILE

GLN

GLU

ASN

GLY

16

GLY

TRP

ASP

THR

PHE

VAL

GLU

LEU

TYR

GLY

17

ASN

ALA

GLU

SER

ARG

LYS

GLY

18

GLN

GLU

ARG

LEU

GLU

HIS

19

HIS

Samples:

sample_1: BCL-xL_apo, [U-100% 13C; U-100% 15N; U-95% 2H; Ile,Leu,Val C1H3], 0.9 mM; sodium phosphate 10 mM; sodium chloride 40 mM; NaN3 0.1%; H2O 92%; D2O 8%

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 273 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 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 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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, peak picking, structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz