BMRB Entry 27133

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27133

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Backbone 1H, 13C and 15N chemical shift assignments for the full length of human uracil DNA glycosylase UNG2
Deposition date:
2017-06-10
Original release date:
2017-09-14
Authors:
Buchinger, Edith; Wiik, Siv; Kusnierczyk, Anna; Rabe, Renana; Aas, Per; Kavli, Bodil; Slupphaug, Geir; Aachmann, Finn
Citation:

Citation: Buchinger, Edith; Wiik, Siv; Kusnierczyk, Anna; Rabe, Renana; Aas, Per; Kavli, Bodil; Slupphaug, Geir; Aachmann, Finn. "Backbone 1H, 13C and 15N chemical shift assignment of full-length human uracil DNA glycosylase UNG2"  Biomol. NMR Assign. 12, 15-22 (2018).
PubMed: 28879561

Assembly members:

Assembly members:
NUNG2, polymer, 119 residues, Formula weight is not available
CUNG2, polymer, 246 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: pTYB12 and pVB-1A0B1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NUNG2: MIGQKTLYSFFSPSPARKRH APSPEPAVQGTGVAGVPEES GDAAAIPAKKAPAGQEEPGT PPSSPLSAEQLDRIQRNKAA ALLRLAARNVPVAAAGSEQK LISEEDLKASGADHHHHHH
CUNG2: MGSSHHHHHHSSGLVPRGSH MIEGRCFGESWKKHLSGEFG KPYFIKLMGFVAEERKHYTV YPPPHQVFTWTQMCDIKDVK VVILGQDPYHGPNQAHGLCF SVQRPVPPPPSLENIYKELS TDIEDFVHPGHGDLSGWAKQ GVLLLNAVLTVRAHQANSHK ERGWEQFTDAVVSWLNQNSN GLVFLLWGSYAQKKGSAIDR KRHHVLQTAHPSPLSVYRGF FGCRHFSKTNELLQKSGKKP IDWKEL

Data typeCount
13C chemical shifts1355
15N chemical shifts516
1H chemical shifts1303

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-terminal UNG21
2C-terminal UNG22

Entities:

Entity 1, N-terminal UNG2 119 residues - Formula weight is not available

A93-H119 is a non-native purification tag that was not included in this upload

1   METILEGLYGLNLYSTHRLEUTYRSERPHE
2   PHESERPROSERPROALAARGLYSARGHIS
3   ALAPROSERPROGLUPROALAVALGLNGLY
4   THRGLYVALALAGLYVALPROGLUGLUSER
5   GLYASPALAALAALAILEPROALALYSLYS
6   ALAPROALAGLYGLNGLUGLUPROGLYTHR
7   PROPROSERSERPROLEUSERALAGLUGLN
8   LEUASPARGILEGLNARGASNLYSALAALA
9   ALALEULEUARGLEUALAALAARGASNVAL
10   PROVALALAALAALAGLYSERGLUGLNLYS
11   LEUILESERGLUGLUASPLEULYSALASER
12   GLYALAASPHISHISHISHISHISHIS

Entity 2, C-terminal UNG2 246 residues - Formula weight is not available

The first 25AA are a non-native purification tag followed by a C26G mutant.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METILEGLUGLYARGCYSPHEGLYGLUSER
4   TRPLYSLYSHISLEUSERGLYGLUPHEGLY
5   LYSPROTYRPHEILELYSLEUMETGLYPHE
6   VALALAGLUGLUARGLYSHISTYRTHRVAL
7   TYRPROPROPROHISGLNVALPHETHRTRP
8   THRGLNMETCYSASPILELYSASPVALLYS
9   VALVALILELEUGLYGLNASPPROTYRHIS
10   GLYPROASNGLNALAHISGLYLEUCYSPHE
11   SERVALGLNARGPROVALPROPROPROPRO
12   SERLEUGLUASNILETYRLYSGLULEUSER
13   THRASPILEGLUASPPHEVALHISPROGLY
14   HISGLYASPLEUSERGLYTRPALALYSGLN
15   GLYVALLEULEULEUASNALAVALLEUTHR
16   VALARGALAHISGLNALAASNSERHISLYS
17   GLUARGGLYTRPGLUGLNPHETHRASPALA
18   VALVALSERTRPLEUASNGLNASNSERASN
19   GLYLEUVALPHELEULEUTRPGLYSERTYR
20   ALAGLNLYSLYSGLYSERALAILEASPARG
21   LYSARGHISHISVALLEUGLNTHRALAHIS
22   PROSERPROLEUSERVALTYRARGGLYPHE
23   PHEGLYCYSARGHISPHESERLYSTHRASN
24   GLULEULEUGLNLYSSERGLYLYSLYSPRO
25   ILEASPTRPLYSGLULEU

Samples:

sample_1: NUNG2, [U-95% 13C; U-95% 15N], 0.2 mM; HEPES 20 mM; sodium chloride 25 mM; Complete protease inhibitor 2 uL

sample_2: NUNG2, [U-95% 13C; U-95% 15N], 0.3 mM; sodium phosphate 20 mM; sodium chloride 10 mM; Complete protease inhibitor 2 uL

sample_3: CUNG2, [U-95% 13C; U-95% 15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 25 mM; Complete protease inhibitor 2 uL; DTT 5 mM

sample_4: CUNG2, [U-95% 13C; U-95% 15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 10 mM; Complete protease inhibitor 2 uL; DTT 5 mM

sample_conditions_1: pH: 6.9; pressure: 1 atm; temperature: 298 K

sample_conditions_2: pH: 7; pressure: 1 atm; temperature: 298 K

sample_conditions_3: pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_4: pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_2
2D CONsample_2isotropicsample_conditions_2
2D CANsample_2isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2
3D CBCA(CO)NHsample_2isotropicsample_conditions_2
3D HN(CO)CAsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_2isotropicsample_conditions_2
3D HCCH-COSYsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_2isotropicsample_conditions_2
2D 1H-15N HSQCsample_3isotropicsample_conditions_3
3D HNCOsample_3isotropicsample_conditions_3
3D HNCAsample_3isotropicsample_conditions_3
3D HN(CO)CAsample_3isotropicsample_conditions_3
3D HN(CA)COsample_3isotropicsample_conditions_3
3D CBCA(CO)NHsample_3isotropicsample_conditions_3
3D HNCACBsample_3isotropicsample_conditions_3
3D HBHA(CO)NHsample_3isotropicsample_conditions_3
3D HBHANHsample_3isotropicsample_conditions_3
2D 1H-15N HSQCsample_4isotropicsample_conditions_4
3D HNCOsample_4isotropicsample_conditions_4
3D HNCAsample_4isotropicsample_conditions_4
3D HN(CO)CAsample_4isotropicsample_conditions_4
3D HNCACBsample_4isotropicsample_conditions_4
3D CBCA(CO)NHsample_4isotropicsample_conditions_4

Software:

CARA, Keller and Wutrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance I 600 MHz
  • Bruker Avance III HD 800 MHz

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