BMRB Entry 26766

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26766

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Title:
1H, 13C and 15N backbone resonance assignment for the 40.5 kDa catalytic domain of Ubiquitin Specific Protease 7 (USP7)
Deposition date:
2016-03-22
Original release date:
2016-08-29
Authors:
Di Lello, Paola; Maurer, Till
Citation:

Citation: Di Lello, Paola; Rouge, Lionel; Pan, Borlan; Maurer, Till. "1H, 13C and 15N backbone resonance assignment for the 40.5 kDa catalytic domain of Ubiquitin Specific Protease 7 (USP7)"  Biomol. NMR Assign. 10, 345-349 (2016).
PubMed: 27386854

Assembly members:

Assembly members:
USP7, polymer, 349 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-15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
USP7: GSKKHTGYVGLKNQGATCYM NSLLQTLFFTNQLRKAVYMM PTEGDDSSKSVPLALQRVFY ELQHSDKPVGTKKLTKSFGW ETLDSFMQHDVQELCRVLLD NVENKMKGTCVEGTIPKLFR GKMVSYIQCKEVDYRSDRRE DYYDIQLSIKGKKNIFESFV DYVAVEQLDGDNKYDAGEHG LQEAEKGVKFLTLPPVLHLQ LMRFMYDPQTDQNIKINDRF EFPEQLPLDEFLQKTDPKDP ANYILHAVLVHSGDNHGGHY VVYLNPKGDGKWCKFDDDVV SRCTKEEAIEHNYGGHDDDL SVRHCTNAYMLVYIRESKLS EVLQAVTDHDIPQQLVERLQ EEKRIEAQK

Data sets:
Data typeCount
13C chemical shifts883
15N chemical shifts279
1H chemical shifts279

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1USP71

Entities:

Entity 1, USP7 349 residues - Formula weight is not available

The first two residues at the N-terminus (i.e. Gly-Ser) are due to cloning artifacts.

1   GLYSERLYSLYSHISTHRGLYTYRVALGLY
2   LEULYSASNGLNGLYALATHRCYSTYRMET
3   ASNSERLEULEUGLNTHRLEUPHEPHETHR
4   ASNGLNLEUARGLYSALAVALTYRMETMET
5   PROTHRGLUGLYASPASPSERSERLYSSER
6   VALPROLEUALALEUGLNARGVALPHETYR
7   GLULEUGLNHISSERASPLYSPROVALGLY
8   THRLYSLYSLEUTHRLYSSERPHEGLYTRP
9   GLUTHRLEUASPSERPHEMETGLNHISASP
10   VALGLNGLULEUCYSARGVALLEULEUASP
11   ASNVALGLUASNLYSMETLYSGLYTHRCYS
12   VALGLUGLYTHRILEPROLYSLEUPHEARG
13   GLYLYSMETVALSERTYRILEGLNCYSLYS
14   GLUVALASPTYRARGSERASPARGARGGLU
15   ASPTYRTYRASPILEGLNLEUSERILELYS
16   GLYLYSLYSASNILEPHEGLUSERPHEVAL
17   ASPTYRVALALAVALGLUGLNLEUASPGLY
18   ASPASNLYSTYRASPALAGLYGLUHISGLY
19   LEUGLNGLUALAGLULYSGLYVALLYSPHE
20   LEUTHRLEUPROPROVALLEUHISLEUGLN
21   LEUMETARGPHEMETTYRASPPROGLNTHR
22   ASPGLNASNILELYSILEASNASPARGPHE
23   GLUPHEPROGLUGLNLEUPROLEUASPGLU
24   PHELEUGLNLYSTHRASPPROLYSASPPRO
25   ALAASNTYRILELEUHISALAVALLEUVAL
26   HISSERGLYASPASNHISGLYGLYHISTYR
27   VALVALTYRLEUASNPROLYSGLYASPGLY
28   LYSTRPCYSLYSPHEASPASPASPVALVAL
29   SERARGCYSTHRLYSGLUGLUALAILEGLU
30   HISASNTYRGLYGLYHISASPASPASPLEU
31   SERVALARGHISCYSTHRASNALATYRMET
32   LEUVALTYRILEARGGLUSERLYSLEUSER
33   GLUVALLEUGLNALAVALTHRASPHISASP
34   ILEPROGLNGLNLEUVALGLUARGLEUGLN
35   GLUGLULYSARGILEGLUALAGLNLYS

Samples:

sample_1: USP7, U-[15 N-13C-2H], 1[13CH3]-Ile, [13CH3]-Leu/Val and [13CH3]-Met, 400 uM

sample_2: USP7, [U-2H] and [U-15N-U-2H]-Cys, 175 uM

sample_3: USP7, [U-2H] and [U-15N]-Arg, 175 uM

sample_4: USP7, [U-2H] and [U-15N]-Lys, 175 uM

sample_5: USP7, [U-2H] and [U-15N]-Val, 175 uM

sample_6: USP7, [U-2H] and [U-15N]-Ile, 175 uM

sample_7: USP7, [U-2H] and [U-15N]-His, 275 uM

sample_8: USP7, [U-2H] and [U-15N]-Met, 225 uM

sample_conditions_1: ionic strength: 163 mM; pH: 7.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D TROSY-HNCOsample_1isotropicsample_conditions_1
3D TROSY-HNCAsample_1isotropicsample_conditions_1
3D TROSY-HNCACBsample_1isotropicsample_conditions_1
3D TROSY-HN(CO)CAsample_1isotropicsample_conditions_1
3D TROSY-HN(CO)CACBsample_1isotropicsample_conditions_1
3D TROSY-HN(CA)COsample_1isotropicsample_conditions_1
3D H(NCA)NNHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_2isotropicsample_conditions_1
2D 1H-15N TROSYsample_3isotropicsample_conditions_1
2D 1H-15N TROSYsample_4isotropicsample_conditions_1
2D 1H-15N TROSYsample_5isotropicsample_conditions_1
2D 1H-15N TROSYsample_6isotropicsample_conditions_1
2D 1H-15N TROSYsample_7isotropicsample_conditions_1
2D 1H-15N TROSYsample_8isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

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