BMRB Entry 51188

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51188

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Title:
Backbone and ILV side chain assignment of the catalytic domain of human deubiquitinating enzyme USP7
Deposition date:
2021-11-23
Original release date:
2021-12-19
Authors:
Korzhnev, Dmitry; Valles, Gabrielle; Pozhidaeva, Alexandra; Bezsonova, Irina
Citation:

Citation: Valles, Gabrielle; Pozhidaeva, Alexandra; Korzhnev, Dmitry; Bezsonova, Irina. "Backbone and ILV side-chain NMR resonance assignments of the catalytic domain of human deubiquitinating enzyme USP7"  Biomol. NMR Assign. 16, 197-203 (2022).
PubMed: 35536398

Assembly members:

Assembly members:
entity_1, polymer, 356 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: pet28a-LIC

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSSKKHTGYVGLKNQGATCY MNSLLQTLFFTNQLRKAVYM MPTEGDDSSKSVPLALQRVF YELQHSDKPVGTKKLTKSFG WETLDSFMQHDVQELCRVLL DNVENKMKGTCVEGTIPKLF RGKMVSYIQCKEVDYRSDRR EDYYDIQLSIKGKKNIFESF VDYVAVEQLDGDNKYDAGEH GLQEAEKGVKFLTLPPVLHL QLMRFMYDPQTDQNIKINDR FEFPEQLPLDEFLQKTDPKD PANYILHAVLVHSGDNHGGH YVVYLNPKGDGKWCKFDDDV VSRCTKEEAIEHNYGGHDDD LSVRHCTNAYMLVYIRESKL SEVLQAVTDHDIPQQLVERL QEEKRIEAQKRKERQE

Data typeCount
13C chemical shifts1135
15N chemical shifts315
1H chemical shifts690

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1USP71

Entities:

Entity 1, USP7 356 residues - Formula weight is not available

1   GLYSERSERLYSLYSHISTHRGLYTYRVAL
2   GLYLEULYSASNGLNGLYALATHRCYSTYR
3   METASNSERLEULEUGLNTHRLEUPHEPHE
4   THRASNGLNLEUARGLYSALAVALTYRMET
5   METPROTHRGLUGLYASPASPSERSERLYS
6   SERVALPROLEUALALEUGLNARGVALPHE
7   TYRGLULEUGLNHISSERASPLYSPROVAL
8   GLYTHRLYSLYSLEUTHRLYSSERPHEGLY
9   TRPGLUTHRLEUASPSERPHEMETGLNHIS
10   ASPVALGLNGLULEUCYSARGVALLEULEU
11   ASPASNVALGLUASNLYSMETLYSGLYTHR
12   CYSVALGLUGLYTHRILEPROLYSLEUPHE
13   ARGGLYLYSMETVALSERTYRILEGLNCYS
14   LYSGLUVALASPTYRARGSERASPARGARG
15   GLUASPTYRTYRASPILEGLNLEUSERILE
16   LYSGLYLYSLYSASNILEPHEGLUSERPHE
17   VALASPTYRVALALAVALGLUGLNLEUASP
18   GLYASPASNLYSTYRASPALAGLYGLUHIS
19   GLYLEUGLNGLUALAGLULYSGLYVALLYS
20   PHELEUTHRLEUPROPROVALLEUHISLEU
21   GLNLEUMETARGPHEMETTYRASPPROGLN
22   THRASPGLNASNILELYSILEASNASPARG
23   PHEGLUPHEPROGLUGLNLEUPROLEUASP
24   GLUPHELEUGLNLYSTHRASPPROLYSASP
25   PROALAASNTYRILELEUHISALAVALLEU
26   VALHISSERGLYASPASNHISGLYGLYHIS
27   TYRVALVALTYRLEUASNPROLYSGLYASP
28   GLYLYSTRPCYSLYSPHEASPASPASPVAL
29   VALSERARGCYSTHRLYSGLUGLUALAILE
30   GLUHISASNTYRGLYGLYHISASPASPASP
31   LEUSERVALARGHISCYSTHRASNALATYR
32   METLEUVALTYRILEARGGLUSERLYSLEU
33   SERGLUVALLEUGLNALAVALTHRASPHIS
34   ASPILEPROGLNGLNLEUVALGLUARGLEU
35   GLNGLUGLULYSARGILEGLUALAGLNLYS
36   ARGLYSGLUARGGLNGLU

Samples:

sample_1: USP7, [U-15N; U-2H; U-13C], 1 mM; TRIS HCL 20 mM; NaCl 100 mM; DTT 2 mM

sample_conditions_1: ionic strength: 120 mM; pH: 7.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
2D 1H-13C TROSY-HMQCsample_1isotropicsample_conditions_1
HMCMCGCBCACOsample_1isotropicsample_conditions_1
HMCMCGCBCAsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Agilent VXRS 800 MHz

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