BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 26901

Title: 1H, 13C and 15N backbone and side-chain resonance assignments of the ZnF UBP domain of USP20/VDU2   PubMed: 28091961

Deposition date: 2016-09-19 Original release date: 2017-02-15

Authors: Yang, Yuanyuan; Wen, Yi; Zhang, Naixia

Citation: Yang, Yuanyuan; Wen, Yi; Zhang, Naixia. "1H, 13C and 15N backbone and side-chain resonance assignments of the ZnF-UBP domain of USP20/VDU2"  Biomol. NMR Assign. 11, 91-93 (2017).

Assembly members:
USP20, polymer, 102 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
USP20: GSHMGDSRDLCPHLDSIGEV TKEDLLLKSKGTCQSCGVTG PNLWACLQVACPYVGCGESF ADHSTIHAQAKKHNLTVNLT TFRLWCYACEKEVFLEQRLA AP

Data sets:
Data typeCount
13C chemical shifts389
15N chemical shifts95
1H chemical shifts589

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1USP201

Entities:

Entity 1, USP20 102 residues - Formula weight is not available

1   GLYSERHISMETGLYASPSERARGASPLEU
2   CYSPROHISLEUASPSERILEGLYGLUVAL
3   THRLYSGLUASPLEULEULEULYSSERLYS
4   GLYTHRCYSGLNSERCYSGLYVALTHRGLY
5   PROASNLEUTRPALACYSLEUGLNVALALA
6   CYSPROTYRVALGLYCYSGLYGLUSERPHE
7   ALAASPHISSERTHRILEHISALAGLNALA
8   LYSLYSHISASNLEUTHRVALASNLEUTHR
9   THRPHEARGLEUTRPCYSTYRALACYSGLU
10   LYSGLUVALPHELEUGLUGLNARGLEUALA
11   ALAPRO

Samples:

sample_1: D2O 10%; H2O 90%; USP20, [U-100% 13C; U-100% 15N], 0.6 – 0.8 mM; Na2HPO4/NaH2PO4 20 mM; NaCl 100 mM; DTT 2 mM; ZnSO4 50 uM

sample_2: D2O 100%; USP20, [U-100% 13C; U-100% 15N], 0.6 – 0.8 mM; Na2HPO4/NaH2PO4 20 mM; NaCl 100 mM; DTT 2 mM; ZnSO4 50 uM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298.2 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts