BMRB Entry 26901

Name: 1H, 13C and 15N backbone and side-chain resonance assignments of the ZnF UBP domain of USP20/VDU2
Published: 2017-02-15

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26901

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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:

1H, 13C and 15N backbone and side-chain resonance assignments of the ZnF UBP domain of USP20/VDU2

Deposition date:

2016-09-19

Original release date:

2017-02-15

Authors:

Yang, Yuanyuan; Wen, Yi; Zhang, Naixia

Citation:

Citation: Yang, Yuanyuan; Wen, Yi; Zhang, Naixia. "1H, 13C and 15N backbone and side-chain resonance assignments of the ZnF-UBP domain of USP20/VDU2" Biomol. NMR Assign. 11, 91-93 (2017).
PubMed: 28091961

Assembly members:

Assembly members:
USP20, polymer, 102 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: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
USP20: GSHMGDSRDLCPHLDSIGEV TKEDLLLKSKGTCQSCGVTG PNLWACLQVACPYVGCGESF ADHSTIHAQAKKHNLTVNLT TFRLWCYACEKEVFLEQRLA AP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	389
15N chemical shifts	95
1H chemical shifts	589

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	USP20	1

Entities:

Entity 1, USP20 102 residues - Formula weight is not available

1

GLY

SER

HIS

MET

GLY

ASP

SER

ARG

ASP

LEU

2

CYS

PRO

HIS

LEU

ASP

SER

ILE

GLY

GLU

VAL

3

THR

LYS

GLU

ASP

LEU

LYS

SER

LYS

4

GLY

THR

CYS

GLN

SER

CYS

GLY

VAL

THR

GLY

5

PRO

ASN

LEU

TRP

ALA

CYS

LEU

GLN

VAL

ALA

6

CYS

PRO

TYR

VAL

GLY

CYS

GLY

GLU

SER

PHE

7

ALA

ASP

HIS

SER

THR

ILE

HIS

ALA

GLN

ALA

8

LYS

HIS

ASN

LEU

THR

VAL

ASN

LEU

THR

9

THR

PHE

ARG

LEU

TRP

CYS

TYR

ALA

CYS

GLU

10

LYS

GLU

VAL

PHE

LEU

GLU

GLN

ARG

LEU

ALA

11

ALA

PRO

Samples:

sample_1: D2O 10%; H2O 90%; USP20, [U-100% 13C; U-100% 15N], 0.6 – 0.8 mM; Na2HPO4/NaH2PO4 20 mM; NaCl 100 mM; DTT 2 mM; ZnSO4 50 uM

sample_2: D2O 100%; USP20, [U-100% 13C; U-100% 15N], 0.6 – 0.8 mM; Na2HPO4/NaH2PO4 20 mM; NaCl 100 mM; DTT 2 mM; ZnSO4 50 uM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298.2 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	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 HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

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