BMRB Entry 50276

Name: Backbone Assignments for human BCL-XL(1-212)
Published: 2020-09-18

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50276

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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:

Backbone Assignments for human BCL-XL(1-212)

Deposition date:

2020-05-15

Original release date:

2020-09-18

Authors:

Ryzhov, Pavel; Yao, Yong; Marassi, Francesca

Citation:

Citation: Ryzhov, Pavel; Tian, Ye; Yao, Yong; Bobkov, Andrey; Im, Wonpil; Marassi, Francesca. "Conformational States of the Cytoprotective Protein Bcl-xL" Biophys. J. 119, 1324-1334 (2020).
PubMed: 32888404

Assembly members:

Assembly members:
entity_1, polymer, 233 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: PET21b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSQSNRELVVDFLSYKLSQK GYSWSQFSDVEENRTEAPEG TESEMETPSAINGNPSWHLA DSPAVNGATGHSSSLDAREV IPMAAVKQALREAGDEFELR YRRAFSDLTSQLHITPGTAY QSFEQVVNELFRDGVNWGRI VAFFSFGGALCVESVDKEMQ VLVSRIAAWMATYLNDHLEP WIQENGGWDTFVELYGNNAA AESRKGQERFNRWFLTGMTV AGVVLLGSLFSRK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	293
15N chemical shifts	179
1H chemical shifts	179

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BCL-XL	1

Entities:

Entity 1, BCL-XL 233 residues - Formula weight is not available

1

MET

SER

GLN

SER

ASN

ARG

GLU

LEU

VAL

2

ASP

PHE

LEU

SER

TYR

LYS

LEU

SER

GLN

LYS

3

GLY

TYR

SER

TRP

SER

GLN

PHE

SER

ASP

VAL

4

GLU

ASN

ARG

THR

GLU

ALA

PRO

GLU

GLY

5

THR

GLU

SER

GLU

MET

GLU

THR

PRO

SER

ALA

6

ILE

ASN

GLY

ASN

PRO

SER

TRP

HIS

LEU

ALA

7

ASP

SER

PRO

ALA

VAL

ASN

GLY

ALA

THR

GLY

8

HIS

SER

LEU

ASP

ALA

ARG

GLU

VAL

9

ILE

PRO

MET

ALA

VAL

LYS

GLN

ALA

LEU

10

ARG

GLU

ALA

GLY

ASP

GLU

PHE

GLU

LEU

ARG

11

TYR

ARG

ALA

PHE

SER

ASP

LEU

THR

SER

12

GLN

LEU

HIS

ILE

THR

PRO

GLY

THR

ALA

TYR

13

GLN

SER

PHE

GLU

GLN

VAL

ASN

GLU

LEU

14

PHE

ARG

ASP

GLY

VAL

ASN

TRP

GLY

ARG

ILE

15

VAL

ALA

PHE

SER

PHE

GLY

ALA

LEU

16

CYS

VAL

GLU

SER

VAL

ASP

LYS

GLU

MET

GLN

17

VAL

LEU

VAL

SER

ARG

ILE

ALA

TRP

MET

18

ALA

THR

TYR

LEU

ASN

ASP

HIS

LEU

GLU

PRO

19

TRP

ILE

GLN

GLU

ASN

GLY

TRP

ASP

THR

20

PHE

VAL

GLU

LEU

TYR

GLY

ASN

ALA

21

ALA

GLU

SER

ARG

LYS

GLY

GLN

GLU

ARG

PHE

22

ASN

ARG

TRP

PHE

LEU

THR

GLY

MET

THR

VAL

23

ALA

GLY

VAL

LEU

GLY

SER

LEU

PHE

24

SER

ARG

LYS

Samples:

sample_1: BCL-XL, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 20 mM; DTT 2 mM; EDTA 1 mM

sample_conditions_1: ionic strength: 0.025 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - processing

NMRViewJ - data analysis

NMR spectrometers:

Bruker Avance 600 MHz

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