BMRB Entry 12039

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR12039

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

Title:
Backbone assignment for the segmental-labeled basic region and HMG-box in the phosphorylated DNA-binding domain of Drosophila melanogaster SSRP1
Deposition date:
2019-10-28
Original release date:
2020-07-09
Authors:
Aoki, Daisuke; Uewaki, Jun-ichi; Tochio, Naoya; Tate, Shin-ichi
Citation:

Citation: Aoki, Daisuke; Awazu, Akinori; Fujii, Masashi; Uewaki, Jun-ichi; Hashimoto, Manami; Tochio, Naoya; Umehara, Takashi; Tate, Shin-ichi. "Ultrasensitive Change in Nucleosome Binding by Multiple Phosphorylations to the Intrinsically Disordered Region of the Histone Chaperone FACT."  J. Mol. Biol. ., .-. (2020).
PubMed: 32553729

Assembly members:

Assembly members:
BID-HMG, polymer, 192 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: fruit fly   Taxonomy ID: 7227   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Drosophila melanogaster

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pTWIN1-his and pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BID-HMG: MGYKDVDFGDSDNENEPDAY LARLKAEAREKEEDDDDGDS DEESTDEDFKPNENESDVAE EYDSNVESDSDDDSDASGGG GDSDGACKKKEKKSEKKEKK EKKHKEKERTKKPSKKKKDS GKPKRATTAFMLWLNDTRES IKRENPGIKVTEIAKKGGEM WKELKDKSKWEDAAAKDKQR YHDEMRNYKPEA

Data sets:
Data typeCount
13C chemical shifts276
15N chemical shifts89
1H chemical shifts89

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1component 11

Entities:

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

S11, S40, S44, S56, S64, S68, S70 and S74 were phosphorylated by CK2.

1   METGLYTYRLYSASPVALASPPHEGLYASP
2   SERASPASNGLUASNGLUPROASPALATYR
3   LEUALAARGLEULYSALAGLUALAARGGLU
4   LYSGLUGLUASPASPASPASPGLYASPSER
5   ASPGLUGLUSERTHRASPGLUASPPHELYS
6   PROASNGLUASNGLUSERASPVALALAGLU
7   GLUTYRASPSERASNVALGLUSERASPSER
8   ASPASPASPSERASPALASERGLYGLYGLY
9   GLYASPSERASPGLYALACYSLYSLYSLYS
10   GLULYSLYSSERGLULYSLYSGLULYSLYS
11   GLULYSLYSHISLYSGLULYSGLUARGTHR
12   LYSLYSPROSERLYSLYSLYSLYSASPSER
13   GLYLYSPROLYSARGALATHRTHRALAPHE
14   METLEUTRPLEUASNASPTHRARGGLUSER
15   ILELYSARGGLUASNPROGLYILELYSVAL
16   THRGLUILEALALYSLYSGLYGLYGLUMET
17   TRPLYSGLULEULYSASPLYSSERLYSTRP
18   GLUASPALAALAALALYSASPLYSGLNARG
19   TYRHISASPGLUMETARGASNTYRLYSPRO
20   GLUALA

Samples:

sample_1: BID-HMG, [U-13C; U-15N], 0.55 mM; TRIS 50 mM; DTT 1 mM; sodium azide 0.03%; D2O, [U-2H], 6%; H2O 94%

sample_conditions_1: ionic strength: 50 mM; pH: 6.6; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Magro, Kobayashi N - data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz

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