BMRB Entry 27696

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27696

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

Title:
NMR assignment of doubly monoubiquitinated p15
Deposition date:
2018-11-20
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:
p15CCSS, polymer, 110 residues, Formula weight is not available
ubiquitin, polymer, 76 residues, 8579.94 Da.

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
p15CCSS: VRTKADSVPGTYRCVVAARA PRCVLGSSTSATNSTSVSSR KAENKYAGGNPVSVRPTPKW QKGIGEFFRLSPKDSEKENQ IPEEAGSSGLGKAKRKASPL QPDHTNDEKE
ubiquitin: MQIFVKTLTGKTITLEVEPS DTIENVKAKIQDKEGIPPDE QRLIFAGKQLQDGRTLSDYN IEKESTLHLVLRLRGG

Data sets:
Data typeCount
13C chemical shifts318
15N chemical shifts99
1H chemical shifts209

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1p15CCSS1
2ubiquitin, 12
3ubiquitin, 22

Entities:

Entity 1, p15CCSS 110 residues - Formula weight is not available

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

Entity 2, ubiquitin, 1 76 residues - 8579.94 Da.

1   METGLNILEPHEVALLYSTHRLEUTHRGLY
2   LYSTHRILETHRLEUGLUVALGLUPROSER
3   ASPTHRILEGLUASNVALLYSALALYSILE
4   GLNASPLYSGLUGLYILEPROPROASPGLU
5   GLNARGLEUILEPHEALAGLYLYSGLNLEU
6   GLNASPGLYARGTHRLEUSERASPTYRASN
7   ILEGLULYSGLUSERTHRLEUHISLEUVAL
8   LEUARGLEUARGGLYGLY

Samples:

sample_1: dmUbp15, [U-100% 13C; U-100% 15N], 150 uM; DSS 50 uM; sodium phosphate 10 mM; sodium chloride 140 mM; sodium azide 0.01%

sample_conditions_1: ionic strength: 150 mM; 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 HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(COCA)HAsample_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