BMRB Entry 27287

Title:
Catalytic Domain of Human Aprataxin
Deposition date:
2017-10-18
Original release date:
2018-07-17
Authors:
Mueller, Geoffrey; Tumbale, Percy; Schellenberg, Matthew; Williams, Scott; London, Robert
Citation:

Citation: Tumbale, Percy; Schellenberg, Matthew; Mueller, Geoffrey; Fairweather, Emma; Watson, Mandy; Little, Jessica; Krahn, Juno; Waddell, Ian; London, Robert; Williams, R Scott. "Mechanism of APTX nicked DNA sensing and pleiotropic inactivation in neurodegenerative disease"  EMBO J. 37, e98875-e98875 (2018).
PubMed: 29934293

Assembly members:

Assembly members:
hAPTX, polymer, 192 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: pET

Data sets:
Data typeCount
13C chemical shifts312
15N chemical shifts149
1H chemical shifts149

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1APTX1

Entities:

Entity 1, APTX 192 residues - Formula weight is not available

1   GLYSERHISMETLYSASPALAPROILELYS
2   LYSGLUSERLEUGLYHISTRPSERGLNGLY
3   LEULYSILESERMETGLNASPPROLYSMET
4   GLNVALTYRLYSASPGLUGLNVALVALVAL
5   ILELYSASPLYSTYRPROLYSALAARGTYR
6   HISTRPLEUVALLEUPROTRPTHRSERILE
7   SERSERLEULYSALAVALALAARGGLUHIS
8   LEUGLULEULEULYSHISMETHISTHRVAL
9   GLYGLULYSVALILEVALASPPHEALAGLY
10   SERSERLYSLEUARGPHEARGLEUGLYTYR
11   HISALAILEPROSERMETSERHISVALHIS
12   LEUHISVALILESERGLNASPPHEASPSER
13   PROCYSLEULYSASNLYSLYSHISTRPASN
14   SERPHEASNTHRGLUTYRPHELEUGLUSER
15   GLNALAVALILEGLUMETVALGLNGLUALA
16   GLYARGVALTHRVALARGASPGLYMETPRO
17   GLULEULEULYSLEUPROLEUARGCYSHIS
18   GLUCYSGLNGLNLEULEUPROSERILEPRO
19   GLNLEULYSGLUHISLEUARGLYSHISTRP
20   THRGLN

Samples:

sample_1: hAPTX, [U-100% 13C; U-100% 15N], 1 mM; Na phosphate NaH2PO4 5 mM; KCl 1.3 mM; NaCl 67 mM; K phosphate KH2PO4 0.8 mM

sample_conditions_1: ionic strength: 0.075 M; pH: 7.4; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz

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