BMRB Entry 27529

Title:
backbone resonance assignment of USP7 UBL45 domains (residues 884-1102)
Deposition date:
2018-06-27
Original release date:
2018-07-19
Authors:
Bezsonova, Irina; Eldirany, Sherif; Pozhidaeva, Alexandra
Citation:

Citation: Eldirany, Sherif; Pozhidaeva, Alexandra; Bezsonova, Irina. "NMR resonance assignment of ubiquitin specific protease 7 (USP7)."  .

Assembly members:

Assembly members:
USP7, polymer, 220 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: pet15b

Data sets:
Data typeCount
13C chemical shifts472
15N chemical shifts169
1H chemical shifts167

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1USP7 UBL451

Entities:

Entity 1, USP7 UBL45 220 residues - Formula weight is not available

1   GLYLYSILETHRASPPHEGLUASNARGARG
2   SERPHELYSCYSILETRPLEUASNSERGLN
3   PHEARGGLUGLUGLUILETHRLEUTYRPRO
4   ASPLYSHISGLYCYSVALARGASPLEULEU
5   GLUGLUCYSLYSLYSALAVALGLULEUGLY
6   GLULYSALASERGLYLYSLEUARGLEULEU
7   GLUILEVALSERTYRLYSILEILEGLYVAL
8   HISGLNGLUASPGLULEULEUGLUCYSLEU
9   SERPROALATHRSERARGTHRPHEARGILE
10   GLUGLUILEPROLEUASPGLNVALASPILE
11   ASPLYSGLUASNGLUMETLEUVALTHRVAL
12   ALAHISPHEHISLYSGLUVALPHEGLYTHR
13   PHEGLYILEPROPHELEULEUARGILEHIS
14   GLNGLYGLUHISPHEARGGLUVALMETLYS
15   ARGILEGLNSERLEULEUASPILEGLNGLU
16   LYSGLUPHEGLULYSPHELYSPHEALAILE
17   VALMETMETGLYARGHISGLNTYRILEASN
18   GLUASPGLUTYRGLUVALASNLEULYSASP
19   PHEGLUPROGLNPROGLYASNMETSERHIS
20   PROARGPROTRPLEUGLYLEUASPHISPHE
21   ASNLYSALAPROLYSARGSERARGTYRTHR
22   TYRLEUGLULYSALAILELYSILEHISASN

Samples:

sample_1: USP7, [U-100% 13C; U-100% 15N], 0.9 mM; sodium phosphate 50 mM; potassium chloride 150 mM; DTT 2 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 7; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

ccpNMR_Analysis, CCPN - chemical shift assignment

NMR spectrometers:

  • Varian 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