BMRB Entry 27698

Title:
p15CCSS
Deposition date:
2018-11-21
Original release date:
2019-09-24
Authors:
Blanco, Francisco; Ibanez de Opakua, Alain; Gonzalez-magana, Amaia
Citation:

Citation: Gonzalez-Magana, Amaia; de Opakua, Alain Ibanez; Merino, Nekane; Monteiro, Hugo; Diercks, Tammo; Murciano-Calles, Javier; Luque, Irene; Bernado, Pau; Cordeiro, Tiago; Biasio, Alfredo De; Blanco, Francisco. "Double Monoubiquitination Modifies the Molecular Recognition Properties of p15PAF Promoting Binding to the Reader Module of Dnmt1"  ACS Chem. Biol. 14, 2315-2326 (2019).
PubMed: 31479228

Assembly members:

Assembly members:
p15CSS, polymer, 110 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: pET11d

Data sets:
Data typeCount
13C chemical shifts208
15N chemical shifts99
1H chemical shifts99

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1p15CSS1

Entities:

Entity 1, p15CSS 110 residues - Formula weight is not available

The protein lacks the initial methionine and thus it starts with Val2.

1   VALARGTHRLYSALAASPSERVALPROGLY
2   THRTYRARGCYSVALVALALAALAARGALA
3   PROARGCYSVALLEUGLYSERSERTHRSER
4   ALATHRASNSERTHRSERVALSERSERARG
5   LYSALAGLUASNLYSTYRALAGLYGLYASN
6   PROVALSERVALARGPROTHRPROLYSTRP
7   GLNLYSGLYILEGLYGLUPHEPHEARGLEU
8   SERPROLYSASPSERGLULYSGLUASNGLN
9   ILEPROGLUGLUALAGLYSERSERGLYLEU
10   GLYLYSALALYSARGLYSALASERPROLEU
11   GLNPROASPHISTHRASNASPGLULYSGLU

Samples:

sample_1: p15CSS, [U-100% 13C; U-100% 15N], 50 uM; D2O, [U-100% 2H], 5%; DTT 1 mM; sodium azide 0.01%; DSS 50 uM; sodium phosphate 10 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.2; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

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