BMRB Entry 27080

Name: Backbone resonance assignment of the Human Uracil DNA Glycosylase-2
Published: 2017-10-04

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR27080

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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 resonance assignment of the Human Uracil DNA Glycosylase-2

Deposition date:

2017-04-20

Original release date:

2017-10-04

Authors:

Kara, Hesna; Ponchon, Luc; Bouaziz, Serge

Citation:

Citation: Kara, Hesna; Ponchon, Luc; Bouaziz, Serge. "Backbone resonance assignment of the Human Uracil DNA Glycosylase-2" Biomol. NMR Assignments 12, 37-42 (2018).
PubMed: 28940147

Assembly members:

Assembly members:
UNG2, polymer, 248 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
UNG2: MGSSHHHHHHSSGLVPRGSH MENLYFQGFGESWKKHLSGE FGKPYFIKLMGFVAEERKHY TVYPPPHQVFTWTQMCDIKD VKVVILGQDPYHGPNQAHGL CFSVQRPVPPPPSLENIYKE LSTDIEDFVHPGHGDLSGWA KQGVLLLNAVLTVRAHQANS HKERGWEQFTDAVVSWLNQN SNGLVFLLWGSYAQKKGSAI DRKRHHVLQTAHPSPLSVYR GFFGCRHFSKTNELLQKSGK KPIDWKEL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	692
15N chemical shifts	231
1H chemical shifts	231

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	UNG2	1

Entities:

Entity 1, UNG2 248 residues - Formula weight is not available

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

GLU

ASN

LEU

TYR

PHE

GLN

GLY

PHE

GLY

4

GLU

SER

TRP

LYS

HIS

LEU

SER

GLY

GLU

5

PHE

GLY

LYS

PRO

TYR

PHE

ILE

LYS

LEU

MET

6

GLY

PHE

VAL

ALA

GLU

ARG

LYS

HIS

TYR

7

THR

VAL

TYR

PRO

HIS

GLN

VAL

PHE

8

THR

TRP

THR

GLN

MET

CYS

ASP

ILE

LYS

ASP

9

VAL

LYS

VAL

ILE

LEU

GLY

GLN

ASP

PRO

10

TYR

HIS

GLY

PRO

ASN

GLN

ALA

HIS

GLY

LEU

11

CYS

PHE

SER

VAL

GLN

ARG

PRO

VAL

PRO

12

PRO

SER

LEU

GLU

ASN

ILE

TYR

LYS

GLU

13

LEU

SER

THR

ASP

ILE

GLU

ASP

PHE

VAL

HIS

14

PRO

GLY

HIS

GLY

ASP

LEU

SER

GLY

TRP

ALA

15

LYS

GLN

GLY

VAL

LEU

ASN

ALA

VAL

16

LEU

THR

VAL

ARG

ALA

HIS

GLN

ALA

ASN

SER

17

HIS

LYS

GLU

ARG

GLY

TRP

GLU

GLN

PHE

THR

18

ASP

ALA

VAL

SER

TRP

LEU

ASN

GLN

ASN

19

SER

ASN

GLY

LEU

VAL

PHE

LEU

TRP

GLY

20

SER

TYR

ALA

GLN

LYS

GLY

SER

ALA

ILE

21

ASP

ARG

LYS

ARG

HIS

VAL

LEU

GLN

THR

22

ALA

HIS

PRO

SER

PRO

LEU

SER

VAL

TYR

ARG

23

GLY

PHE

GLY

CYS

ARG

HIS

PHE

SER

LYS

24

THR

ASN

GLU

LEU

GLN

LYS

SER

GLY

LYS

25

LYS

PRO

ILE

ASP

TRP

LYS

GLU

LEU

Samples:

sample_1: UNG2, [U-100% 13C; U-100% 15N], 0.4 mM; potassium phosphate 40 mM; DTT 5 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

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

Software:

TOPSPIN v3.5, Bruker - acquisition, processing

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 900 MHz

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