BMRB Entry 26782

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26782

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for human USP7 in complex with ICP0 from HSV-1
Deposition date:
2016-04-21
Original release date:
2016-05-24
Authors:
Pozhidaeva, Alexandra; Korzhnev, Dmitry; Bezsonova, Irina
Citation:

Citation: Pozhidaeva, Alexandra; Mohni, Kareem; Dhe-Paganon, Sirano; Arrowsmith, Cheryl; Weller, Sandra; Korzhnev, Dmitry; Bezsonova, Irina. ""Structural Characterization of Interaction between Human Ubiquitin-specific Protease 7 and Immediate-Early Protein ICP0 of Herpes Simplex Virus-1""  J. Biol. Chem. 290, 22907-22918 (2015).
PubMed: 26224631

Assembly members:

Assembly members:
USP7, polymer, 244 residues, Formula weight is not available
ICP0, polymer, 11 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: humans   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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
USP7: GMDIPQQLVERLQEEKRIEA QKRKERQEAHLYMQVQIVAE DQFCGHQGNDMYDEEKVKYT VFKVLKNSSLAEFVQSLSQT MGFPQDQIRLWPMQARSNGT KRPAMLDNEADGNKTMIELS DNENPWTIFLETVDPELAAS GATLPKFDKDHDVMLFLKMY DPKTRSLNYCGHIYTPISCK IRDLLPVMCDRAGFIQDTSL ILYEEVKPNLTERIQDYDVS LDKALDELMDGDIIVFQKDD PEND
ICP0: GPRKCARKTRH

Data sets:
Data typeCount
13C chemical shifts563
15N chemical shifts187
1H chemical shifts187

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1USP71
2ICP02

Entities:

Entity 1, USP7 244 residues - Formula weight is not available

1   GLYMETASPILEPROGLNGLNLEUVALGLU
2   ARGLEUGLNGLUGLULYSARGILEGLUALA
3   GLNLYSARGLYSGLUARGGLNGLUALAHIS
4   LEUTYRMETGLNVALGLNILEVALALAGLU
5   ASPGLNPHECYSGLYHISGLNGLYASNASP
6   METTYRASPGLUGLULYSVALLYSTYRTHR
7   VALPHELYSVALLEULYSASNSERSERLEU
8   ALAGLUPHEVALGLNSERLEUSERGLNTHR
9   METGLYPHEPROGLNASPGLNILEARGLEU
10   TRPPROMETGLNALAARGSERASNGLYTHR
11   LYSARGPROALAMETLEUASPASNGLUALA
12   ASPGLYASNLYSTHRMETILEGLULEUSER
13   ASPASNGLUASNPROTRPTHRILEPHELEU
14   GLUTHRVALASPPROGLULEUALAALASER
15   GLYALATHRLEUPROLYSPHEASPLYSASP
16   HISASPVALMETLEUPHELEULYSMETTYR
17   ASPPROLYSTHRARGSERLEUASNTYRCYS
18   GLYHISILETYRTHRPROILESERCYSLYS
19   ILEARGASPLEULEUPROVALMETCYSASP
20   ARGALAGLYPHEILEGLNASPTHRSERLEU
21   ILELEUTYRGLUGLUVALLYSPROASNLEU
22   THRGLUARGILEGLNASPTYRASPVALSER
23   LEUASPLYSALALEUASPGLULEUMETASP
24   GLYASPILEILEVALPHEGLNLYSASPASP
25   PROGLUASNASP

Entity 2, ICP0 11 residues - Formula weight is not available

1   GLYPROARGLYSCYSALAARGLYSTHRARG
2   HIS

Samples:

sample_1: USP7, [U-100% 13C; U-100% 15N; U-80% 2H], 0.59 mM; ICP0 4.13 mM; potassium phosphate 20 mM; sodium chloride 100 mM; DTT 2 mM; sodium azide 0.05%; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

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

CcpNmr_Analysis, Vranken, Boucher, Stevens, Fogh, Pajon, Llinas, Ulrich, Markley, Ionides and Laue - chemical shift assignment, data analysis, peak picking

VNMRJ, Varian - collection

NMR spectrometers:

  • Agilent INOVA 800 MHz

Related Database Links:

NCBI NP_003461.2

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