BMRB Entry 27495

Name: Backbone 1H, 13C, 15N chemical shifts of deubiquitinase A phosphorylated at Ser177
Published: 2020-02-28

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27495

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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 1H, 13C, 15N chemical shifts of deubiquitinase A phosphorylated at Ser177

Deposition date:

2018-05-29

Original release date:

2020-02-28

Authors:

Kabra, Ashish; Benson, Catherine; Li, Ying

Citation:

Citation: Kabra, Ashish; Benson, Catherine; Li, Ying. "Backbone 1 H, 13 C, and 15 N resonance assignments of deubiquitinase A in non-phosphorylated and phosphorylated forms" Biomol. NMR Assign. 13, 37-42 (2019).
PubMed: 30232733

Assembly members:

Assembly members:
phosphorylated_DUBA, polymer, 168 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: pET28-MHL

Entity Sequences (FASTA):

Entity Sequences (FASTA):
phosphorylated_DUBA: GAGYNXEDEYEAAAARIEAM DPATVEQQEHWFEKALRDKK GFIIKQMKEDGACLFRAVAD QVYGDQDMHEVVRKHCMDYL MKNADYFSNYVTEDFTTYIN RKRKNNCHGNHIEMQAMAEM YNRPVEVYQYSTEPINTFHG IHQNEDEPIRVSYHRNIHYN SVVNPNKA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	365
15N chemical shifts	116
1H chemical shifts	116

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	phosphorylated DUBA	1

Entities:

Entity 1, phosphorylated DUBA 168 residues - Formula weight is not available

1

GLY

ALA

GLY

TYR

ASN

SEP

GLU

ASP

GLU

TYR

2

GLU

ALA

ARG

ILE

GLU

ALA

MET

3

ASP

PRO

ALA

THR

VAL

GLU

GLN

GLU

HIS

4

TRP

PHE

GLU

LYS

ALA

LEU

ARG

ASP

LYS

5

GLY

PHE

ILE

LYS

GLN

MET

LYS

GLU

ASP

6

GLY

ALA

CYS

LEU

PHE

ARG

ALA

VAL

ALA

ASP

7

GLN

VAL

TYR

GLY

ASP

GLN

ASP

MET

HIS

GLU

8

VAL

ARG

LYS

HIS

CYS

MET

ASP

TYR

LEU

9

MET

LYS

ASN

ALA

ASP

TYR

PHE

SER

ASN

TYR

10

VAL

THR

GLU

ASP

PHE

THR

TYR

ILE

ASN

11

ARG

LYS

ARG

LYS

ASN

CYS

HIS

GLY

ASN

12

HIS

ILE

GLU

MET

GLN

ALA

MET

ALA

GLU

MET

13

TYR

ASN

ARG

PRO

VAL

GLU

VAL

TYR

GLN

TYR

14

SER

THR

GLU

PRO

ILE

ASN

THR

PHE

HIS

GLY

15

ILE

HIS

GLN

ASN

GLU

ASP

GLU

PRO

ILE

ARG

16

VAL

SER

TYR

HIS

ARG

ASN

ILE

HIS

TYR

ASN

17

SER

VAL

ASN

PRO

ASN

LYS

ALA

Samples:

sample_1: phosphorylated DUBA, [U-13C; U-15N; U-2H], 0.5 mM; sodium phosphate 50 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - data analysis

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

NMR spectrometers:

Varian VNMRS 700 MHz

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