BMRB Entry 19522

Name: Solution Structure of the Complex Between BCL-xL and the p53 Core Domain determined with PRE restraints
Published: 2015-07-24

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PDB ID: 2mej
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19522
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution Structure of the Complex Between BCL-xL and the p53 Core Domain determined with PRE restraints

Deposition date: 2013-09-25 Original release date: 2015-07-24

Authors: Viacava Follis, Ariele; Grace, Christy; Kriwacki, Richard

Citation: Viacava Follis, Ariele; Ou, Li; Llambi, Fabien; Green, Douglas; Kriwacki, Richard. "The DNA Binding Domain is a Promiscuous Interaction Hub that Mediates the Nuclear and Cytoplasmic Functions of p53" Nat. Struct. Biol. ., .-..

Assembly members:
BCL-xL, polymer, 212 residues, 16553.609 Da.
p53, polymer, 214 residues, 22016.141 Da.
ZINC ION, non-polymer, 65.409 Da.

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):
BCL-xL: GHSMSQSNRELVVDFLSYKL SQKGYSWSQFSDVEENRTEA PEGTESEMETPSAINGNPSW HLADSPAVNGATGHSSSLDA REVIPMAAVKQALREAGDEF ELRYRRAFSDLTSQLHITPG TAYQSFEQVVNELFRDGVNW GRIVAFFSFGGALCVESVDK EMQVLVSRIAAWMATYLNDH LEPWIQENGGWDTFVELYGN NAAAESRKGQER
p53: GHSTYQGSYGFRLGFLHSGT AKSVTCTYSPALNKMFCQLA KTCPVQLWVDSTPPPGTRVR AMAIYKQSQHMTEVVRRCPH HERCSDSDGLAPPQHLIRVE GNLRVEYLDDRNTFRHSVVV PYEPPEVGSDCTTIHYNYMC NSSCMGGMNRRPILTIITLE DSSGNLLGRNSFEVRVCACP GRDRRTEEENLRKKGEPHHE LPPGSTKRALSNNT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	646
15N chemical shifts	209
1H chemical shifts	399

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BCL-xL	1
2	p53	2
3	ZINC ION	3

Entities:

Entity 1, BCL-xL 212 residues - 16553.609 Da.

The three N terminal residues constitute the leftover portion of a cleaved 6XHis affinity tag. The construct bears a deletion of the C terminal 22 aminoacids for solubility reasons

1

GLY

HIS

SER

MET

SER

GLN

SER

ASN

ARG

GLU

2

LEU

VAL

ASP

PHE

LEU

SER

TYR

LYS

LEU

3

SER

GLN

LYS

GLY

TYR

SER

TRP

SER

GLN

PHE

4

SER

ASP

VAL

GLU

ASN

ARG

THR

GLU

ALA

5

PRO

GLU

GLY

THR

GLU

SER

GLU

MET

GLU

THR

6

PRO

SER

ALA

ILE

ASN

GLY

ASN

PRO

SER

TRP

7

HIS

LEU

ALA

ASP

SER

PRO

ALA

VAL

ASN

GLY

8

ALA

THR

GLY

HIS

SER

LEU

ASP

ALA

9

ARG

GLU

VAL

ILE

PRO

MET

ALA

VAL

LYS

10

GLN

ALA

LEU

ARG

GLU

ALA

GLY

ASP

GLU

PHE

11

GLU

LEU

ARG

TYR

ARG

ALA

PHE

SER

ASP

12

LEU

THR

SER

GLN

LEU

HIS

ILE

THR

PRO

GLY

13

THR

ALA

TYR

GLN

SER

PHE

GLU

GLN

VAL

14

ASN

GLU

LEU

PHE

ARG

ASP

GLY

VAL

ASN

TRP

15

GLY

ARG

ILE

VAL

ALA

PHE

SER

PHE

GLY

16

GLY

ALA

LEU

CYS

VAL

GLU

SER

VAL

ASP

LYS

17

GLU

MET

GLN

VAL

LEU

VAL

SER

ARG

ILE

ALA

18

ALA

TRP

MET

ALA

THR

TYR

LEU

ASN

ASP

HIS

19

LEU

GLU

PRO

TRP

ILE

GLN

GLU

ASN

GLY

20

TRP

ASP

THR

PHE

VAL

GLU

LEU

TYR

GLY

ASN

21

ASN

ALA

GLU

SER

ARG

LYS

GLY

GLN

22

GLU

ARG

Entity 2, p53 214 residues - 22016.141 Da.

1

GLY

HIS

SER

THR

TYR

GLN

GLY

SER

TYR

GLY

2

PHE

ARG

LEU

GLY

PHE

LEU

HIS

SER

GLY

THR

3

ALA

LYS

SER

VAL

THR

CYS

THR

TYR

SER

PRO

4

ALA

LEU

ASN

LYS

MET

PHE

CYS

GLN

LEU

ALA

5

LYS

THR

CYS

PRO

VAL

GLN

LEU

TRP

VAL

ASP

6

SER

THR

PRO

GLY

THR

ARG

VAL

ARG

7

ALA

MET

ALA

ILE

TYR

LYS

GLN

SER

GLN

HIS

8

MET

THR

GLU

VAL

ARG

CYS

PRO

HIS

9

HIS

GLU

ARG

CYS

SER

ASP

SER

ASP

GLY

LEU

10

ALA

PRO

GLN

HIS

LEU

ILE

ARG

VAL

GLU

11

GLY

ASN

LEU

ARG

VAL

GLU

TYR

LEU

ASP

12

ARG

ASN

THR

PHE

ARG

HIS

SER

VAL

13

PRO

TYR

GLU

PRO

GLU

VAL

GLY

SER

ASP

14

CYS

THR

ILE

HIS

TYR

ASN

TYR

MET

CYS

15

ASN

SER

CYS

MET

GLY

MET

ASN

ARG

16

ARG

PRO

ILE

LEU

THR

ILE

THR

LEU

GLU

17

ASP

SER

GLY

ASN

LEU

GLY

ARG

ASN

18

SER

PHE

GLU

VAL

ARG

VAL

CYS

ALA

CYS

PRO

19

GLY

ARG

ASP

ARG

THR

GLU

ASN

20

LEU

ARG

LYS

GLY

GLU

PRO

HIS

GLU

21

LEU

PRO

GLY

SER

THR

LYS

ARG

ALA

LEU

22

SER

ASN

THR

Entity 3, ZINC ION - Zn - 65.409 Da.

1

ZN

Samples:

p53_assignment: p53, [U-98% 13C; U-98% 15N; U-98% 2H], 0.6 mM; sodium phosphate 10 mM; sodium chloride 40 mM; DTT 5 mM; NaN3 0.01%; H2O 93%; D2O 7%

labeled_p53_BCL-xL: p53, [U-98% 13C; U-98% 15N; U-98% 2H], 0.6 mM; BCL-xL 0.65 mM; H2O 93%; D2O 7%

151MTSL_BCL-xL_ox: p53, [U-98% 15N; U-98% 2H], 0.1 mM; BCL-xL_C151MTSL 0.1 mM; H2O 93%; D2O 7%

151MTSL_BCL-xL_red: p53, [U-98% 15N; U-98% 2H], 0.1 mM; BCL-xL_C151MTSL 0.1 mM; DTT 10 mM; H2O 93%; D2O 7%

122MTSL_BCL-xL_ox: p53, [U-98% 15N; U-98% 2H], 0.1 mM; BCL-xL_C151S_S122C MTSL 0.1 mM; H2O 93%; D2O 7%

122MTSL_BCL-xL_red: p53, [U-98% 15N; U-98% 2H], 0.1 mM; BCL-xL_C151S_S122C MTSL 0.1 mM; DTT 10 mM; H2O 93%; D2O 7%

2MTSL_BCL-xL_ox: p53, [U-98% 15N; U-98% 2H], 0.1 mM; BCL-xL_C151S_S2C MTSL 0.1 mM; H2O 93%; D2O 7%

2MTSL_BCL-xL_red: p53, [U-98% 15N; U-98% 2H], 0.1 mM; BCL-xL_C151S_S2C MTSL 0.1 mM; DTT 10 mM; H2O 93%; D2O 7%

BCL-xL_Co_p53: BCL-xL, [U-98% 15N; U-98% 2H], 0.1 mM; Co_p53 0.1 mM; H2O 93%; D2O 7%

BCL-xL_Zn_p53: BCL-xL, [U-98% 15N; U-98% 2H], 0.1 mM; p53 0.1 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 0.05 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	p53_assignment	isotropic	sample_conditions_1
2D 1H-15N HSQC	labeled_p53_BCL-xL	isotropic	sample_conditions_1
2D 1H-15N HSQC	151MTSL_BCL-xL_ox	isotropic	sample_conditions_1
2D 1H-15N HSQC	151MTSL_BCL-xL_red	isotropic	sample_conditions_1
2D 1H-15N HSQC	122MTSL_BCL-xL_ox	isotropic	sample_conditions_1
2D 1H-15N HSQC	122MTSL_BCL-xL_ox	isotropic	sample_conditions_1
2D 1H-15N HSQC	2MTSL_BCL-xL_ox	isotropic	sample_conditions_1
2D 1H-15N HSQC	2MTSL_BCL-xL_red	isotropic	sample_conditions_1
2D 1H-15N HSQC	BCL-xL_Co_p53	isotropic	sample_conditions_1
2D 1H-15N HSQC	BCL-xL_Zn_p53	isotropic	sample_conditions_1
3D 1H-15N NOESY	labeled_p53_BCL-xL	isotropic	sample_conditions_1
3D HNCA	p53_assignment	isotropic	sample_conditions_1
3D HNCACB	p53_assignment	isotropic	sample_conditions_1
3D HNCO	p53_assignment	isotropic	sample_conditions_1
3D HN(CO)CA	p53_assignment	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	p53_assignment	isotropic	sample_conditions_1
3D HCCH-TOCSY	p53_assignment	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	p53_assignment	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	labeled_p53_BCL-xL	isotropic	sample_conditions_1
2D CBCACO	BCL-xL_Co_p53	isotropic	sample_conditions_1
2D CBCACO	BCL-xL_Zn_p53	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	BCL-xL_Co_p53	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	BCL-xL_Zn_p53	isotropic	sample_conditions_1

GB	CAA80661 AAA51039 AAA82173 AAA82174 AAB17352 AAB17353 BAC16799
BMRB	19520 19521
PDB	1AF3 1BXL 1LXL 1MAZ 1PQ0 1PQ1 1R2D 1R2E 1R2G 1R2H 1R2I 2B48 2BZW 2ME8 2ME9 2MEJ 3CVA 3IHC 3IHD 3IHE 3IHF 3IIG 3IIH 3ILB 3ILC 4HNJ
DBJ	BAB71819 BAB85856 BAE27189 BAE42906 BAE73044
EMBL	CAA04597 CAA57886 CAA58557 CAA80661 CAI56777
REF	NP_001003072 NP_001009226 NP_001009228 NP_001028842 NP_001028844
SP	O77737 P53563 Q07817 Q64373
TPG	DAA23121

Biological Magnetic Resonance Data Bank