BMRB Entry 27425

Name: 1/loop partially truncated Phosphomimetic Bcl-2 mutant
Published: 2019-03-29

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR27425

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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:

1/loop partially truncated Phosphomimetic Bcl-2 mutant

Deposition date:

2018-03-14

Original release date:

2019-03-29

Authors:

Song, Ting; Xue, Zhenyu; Zhang, Zhichao

Citation:

Citation: Song, Ting; Cao, Keke; Fan, Yudan; Zhang, Zhichao; Guo, Zongwei; Zhang, Minhang; Liu, Peng. "Expression and solution NMR study of multi-site phosphomimetic mutant BCL-2 protein." Protein Pept. Lett. 26, 449-457 (2019).
PubMed: 30919764

Assembly members:

Assembly members:
EEE-Bcl-2, polymer, 207 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: PET-28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
EEE-Bcl-2: MAHAGRTGYDNREIVMKYIH YKLSQRGYEWDAGDVGAAPP GAAPAPGIFSSQPGHTPHPA ASRDPVARTSPLQTPAAPGA AAGPALSPVPPVVHLTLRQA GDDFSRRYRRDFAEMSSQLH LTPFTARGRFATVVEELFRD GVNWGRIVAFFEFGGVMCVE SVNREMSPLVDNIALWMTEY LNRHLHTWIQDNGGWDAFVE LYGPSMR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	83
15N chemical shifts	78
1H chemical shifts	78

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EEE-Bcl-2	1

Entities:

Entity 1, EEE-Bcl-2 207 residues - Formula weight is not available

1

MET

ALA

HIS

ALA

GLY

ARG

THR

GLY

TYR

ASP

2

ASN

ARG

GLU

ILE

VAL

MET

LYS

TYR

ILE

HIS

3

TYR

LYS

LEU

SER

GLN

ARG

GLY

TYR

GLU

TRP

4

ASP

ALA

GLY

ASP

VAL

GLY

ALA

PRO

5

GLY

ALA

PRO

ALA

PRO

GLY

ILE

PHE

SER

6

SER

GLN

PRO

GLY

HIS

THR

PRO

HIS

PRO

ALA

7

ALA

SER

ARG

ASP

PRO

VAL

ALA

ARG

THR

SER

8

PRO

LEU

GLN

THR

PRO

ALA

PRO

GLY

ALA

9

ALA

GLY

PRO

ALA

LEU

SER

PRO

VAL

PRO

10

PRO

VAL

HIS

LEU

THR

LEU

ARG

GLN

ALA

11

GLY

ASP

PHE

SER

ARG

TYR

ARG

12

ASP

PHE

ALA

GLU

MET

SER

GLN

LEU

HIS

13

LEU

THR

PRO

PHE

THR

ALA

ARG

GLY

ARG

PHE

14

ALA

THR

VAL

GLU

LEU

PHE

ARG

ASP

15

GLY

VAL

ASN

TRP

GLY

ARG

ILE

VAL

ALA

PHE

16

PHE

GLU

PHE

GLY

VAL

MET

CYS

VAL

GLU

17

SER

VAL

ASN

ARG

GLU

MET

SER

PRO

LEU

VAL

18

ASP

ASN

ILE

ALA

LEU

TRP

MET

THR

GLU

TYR

19

LEU

ASN

ARG

HIS

LEU

HIS

THR

TRP

ILE

GLN

20

ASP

ASN

GLY

TRP

ASP

ALA

PHE

VAL

GLU

21

LEU

TYR

GLY

PRO

SER

MET

ARG

Samples:

sample_1: EEE-Bcl-2, [U-100% 13C; U-100% 15N], 0.5 mM; Tris 20 mM; Nacl 150 mM; DTT-d6 5 mM; NaN3 0.02%

sample_conditions_1: ionic strength: 0.17 M; pH: 7.8; 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 HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - data analysis

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker DRX 800 MHz

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