BMRB Entry 51683

Name: UGT2B17-C terminus
Published: 2023-02-02

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51683

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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:

UGT2B17-C terminus

Deposition date:

2022-11-01

Original release date:

2023-02-02

Authors:

Sulekha, Anamika; Osborne, Michael; Gasiorek, Jadwiga; Borden, Katherine

Citation:

Citation: Sulekha, Anamika; Osborne, Michael; Gasiorek, Jadwiga; Borden, Katherine. "1H, 13C, 15N Backbone and sidechain chemical shift assignments of the C-terminal domain of human UDP-glucuronosyltransferase 2B17 (UGT2B17-C)" Biomol. NMR Assignments 17, 67-73 (2023).
PubMed: 36757531

Assembly members:

Assembly members:
entity_1, polymer, 177 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):
entity_1: GSEFGLHCKPAKPLPKEMEE FVQSSGENGIVVFSLGSMIS NMSEESANMIASALAQIPQK VLWRFDGKKPNTLGSNTRLY KWLPQNDLLGHPKTKAFITH GGTNGIYEAIYHGIPMVGIP LFADQHDNIAHMKAKGAALS VDIRTMSSRDLLNALKSVIN DPIYKENIMKLSRIHHD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	641
15N chemical shifts	145
1H chemical shifts	760

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	UGT2B17-C	1

Entities:

Entity 1, UGT2B17-C 177 residues - Formula weight is not available

1

GLY

SER

GLU

PHE

GLY

LEU

HIS

CYS

LYS

PRO

2

ALA

LYS

PRO

LEU

PRO

LYS

GLU

MET

GLU

3

PHE

VAL

GLN

SER

GLY

GLU

ASN

GLY

ILE

4

VAL

PHE

SER

LEU

GLY

SER

MET

ILE

SER

5

ASN

MET

SER

GLU

SER

ALA

ASN

MET

ILE

6

ALA

SER

ALA

LEU

ALA

GLN

ILE

PRO

GLN

LYS

7

VAL

LEU

TRP

ARG

PHE

ASP

GLY

LYS

PRO

8

ASN

THR

LEU

GLY

SER

ASN

THR

ARG

LEU

TYR

9

LYS

TRP

LEU

PRO

GLN

ASN

ASP

LEU

GLY

10

HIS

PRO

LYS

THR

LYS

ALA

PHE

ILE

THR

HIS

11

GLY

THR

ASN

GLY

ILE

TYR

GLU

ALA

ILE

12

TYR

HIS

GLY

ILE

PRO

MET

VAL

GLY

ILE

PRO

13

LEU

PHE

ALA

ASP

GLN

HIS

ASP

ASN

ILE

ALA

14

HIS

MET

LYS

ALA

LYS

GLY

ALA

LEU

SER

15

VAL

ASP

ILE

ARG

THR

MET

SER

ARG

ASP

16

LEU

ASN

ALA

LEU

LYS

SER

VAL

ILE

ASN

17

ASP

PRO

ILE

TYR

LYS

GLU

ASN

ILE

MET

LYS

18

LEU

SER

ARG

ILE

HIS

ASP

Samples:

sample_1: UGT2B17-C, [U-13C; U-15N], 200 uM; D2O, [U-100% 2H], 7%; DTT, [U-2H], 1 mM; DSS, [U-2H], 1 mM; H2O 93%; sodium azide 0.02%

sample_conditions_1: ionic strength: 0.2 M; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR - chemical shift assignment

DANGLE - data analysis

TOPSPIN - collection

NMR spectrometers:

Bruker AVANCE III 600 MHz

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