BMRB Entry 51913

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51913

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Title:
Backbone 1H, 13C and 15N resonance assignment of the Ubiquitin Specific Protease 7 catalytic domain (residues 208-554) in a complex with small molecule ligand
Deposition date:
2023-04-16
Original release date:
2023-12-05
Authors:
Augustyniak, Wojciech; Pandya, Maya; Cliff, Matthew; Lindner, Ilka; Stinn, Anne; Kahmann, Jan; Temmerman, Koen; Waltho, Jonathan; Watson, Martin
Citation:

Citation: Pandya, Maya; Augustyniak, Wojciech; Cliff, Matthew; Lindner, Ilka; Stinn, Anne; Kahmann, Jan; Temmerman, Koen; Dannatt, Hugh; Waltho, Jonathan; Watson, Martin. "Backbone 1H, 13C and 15N resonance assignment of the ubiquitin specific protease 7 catalytic domain (residues 208-554) in complex with a small molecule ligand"  Biomol. NMR Assign. 18, 33-44 (2024).
PubMed: 38472728

Assembly members:

Assembly members:
entity_1, polymer, 351 residues, 40530 Da.
entity_2, non-polymer, 488.39 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-28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMKKHTGYVGLKNQGATC YMNSLLQTLFFTNQLRKAVY MMPTEGDDSSKSVPLALQRV FYELQHSDKPVGTKKLTKSF GWETLDSFMQHDVQELCRVL LDNVENKMKGTCVEGTIPKL FRGKMVSYIQCKEVDYRSDR REDYYDIQLSIKGKKNIFES FVDYVAVEQLDGDNKYDAGE HGLQEAEKGVKFLTLPPVLH LQLMRFMYDPQTDQNIKIND RFEFPEQLPLDEFLQKTDPK DPANYILHAVLVHSGDNHGG HYVVYLNPKGDGKWCKFDDD VVSRCTKEEAIEHNYGGHDD DLSVRHCTNAYMLVYIRESK LSEVLQAVTDHDIPQQLVER LQEEKRIEAQK

Data sets:
Data typeCount
13C chemical shifts553
15N chemical shifts294
1H chemical shifts294

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ubiquitin Specific Protease 7 catalytic domain (residues 208-554)1
2Compound 212

Entities:

Entity 1, Ubiquitin Specific Protease 7 catalytic domain (residues 208-554) 351 residues - 40530 Da.

1   GLYSERHISMETLYSLYSHISTHRGLYTYR
2   VALGLYLEULYSASNGLNGLYALATHRCYS
3   TYRMETASNSERLEULEUGLNTHRLEUPHE
4   PHETHRASNGLNLEUARGLYSALAVALTYR
5   METMETPROTHRGLUGLYASPASPSERSER
6   LYSSERVALPROLEUALALEUGLNARGVAL
7   PHETYRGLULEUGLNHISSERASPLYSPRO
8   VALGLYTHRLYSLYSLEUTHRLYSSERPHE
9   GLYTRPGLUTHRLEUASPSERPHEMETGLN
10   HISASPVALGLNGLULEUCYSARGVALLEU
11   LEUASPASNVALGLUASNLYSMETLYSGLY
12   THRCYSVALGLUGLYTHRILEPROLYSLEU
13   PHEARGGLYLYSMETVALSERTYRILEGLN
14   CYSLYSGLUVALASPTYRARGSERASPARG
15   ARGGLUASPTYRTYRASPILEGLNLEUSER
16   ILELYSGLYLYSLYSASNILEPHEGLUSER
17   PHEVALASPTYRVALALAVALGLUGLNLEU
18   ASPGLYASPASNLYSTYRASPALAGLYGLU
19   HISGLYLEUGLNGLUALAGLULYSGLYVAL
20   LYSPHELEUTHRLEUPROPROVALLEUHIS
21   LEUGLNLEUMETARGPHEMETTYRASPPRO
22   GLNTHRASPGLNASNILELYSILEASNASP
23   ARGPHEGLUPHEPROGLUGLNLEUPROLEU
24   ASPGLUPHELEUGLNLYSTHRASPPROLYS
25   ASPPROALAASNTYRILELEUHISALAVAL
26   LEUVALHISSERGLYASPASNHISGLYGLY
27   HISTYRVALVALTYRLEUASNPROLYSGLY
28   ASPGLYLYSTRPCYSLYSPHEASPASPASP
29   VALVALSERARGCYSTHRLYSGLUGLUALA
30   ILEGLUHISASNTYRGLYGLYHISASPASP
31   ASPLEUSERVALARGHISCYSTHRASNALA
32   TYRMETLEUVALTYRILEARGGLUSERLYS
33   LEUSERGLUVALLEUGLNALAVALTHRASP
34   HISASPILEPROGLNGLNLEUVALGLUARG
35   LEUGLNGLUGLULYSARGILEGLUALAGLN
36   LYS

Entity 2, Compound 21 - C22H26BrN5O3 - 488.39 Da.

1   1

Samples:

sample_1: Ubiquitin Specific Protease 7 catalytic domain (residues 208-554), [U-100% 13C; U-100% 15N; U-100% 2H (carbon bound)], 0.5 ± 0.05 mM; sodium phosphate 25 ± 1 mM; sodium chloride 100 ± 5 mM; TCEP 5 ± 0.2 mM; sodium azide 0.02 ± 0.001 %; D2O, [U-100% 2H], 10 ± 0.2 %; Compound 21 0.73 ± 0.1 mM; DMSO 1 ± 0.1 %

sample_conditions_1: ionic strength: 0.32 M; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

CARA v1.9.1.7 - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

UNP Q93009
NCBI 7874

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