BMRB Entry 50765

Title:
Assignments of free human Tsg101 UEV domain
Deposition date:
2021-02-16
Original release date:
2023-09-11
Authors:
Moschidi, Danai; Cantrelle, Francois-Xavier; Hanoulle, Xavier
Citation:

Citation: Moschidi, Danai; Cantrelle, Francois-Xavier; Boll, Emmanuelle; Hanoulle, Xavier. "Backbone NMR resonance assignment of the apo human Tsg101-UEV domain"  Biomol. NMR Assignm. 17, 49-54 (2023).
PubMed: 36740661

Assembly members:

Assembly members:
entity_1, polymer, 147 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

Data sets:
Data typeCount
13C chemical shifts441
15N chemical shifts156
1H chemical shifts308

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Tsg101_UEV1

Entities:

Entity 1, Tsg101_UEV 147 residues - Formula weight is not available

The author sequence numbering is the Uniprot Q99816 numbering without the 2 first residues from polymer sequence due to cloning tag.

1   GLYALAMETALAVALSERGLUSERGLNLEU
2   LYSLYSMETVALSERLYSTYRLYSTYRARG
3   ASPLEUTHRVALARGGLUTHRVALASNVAL
4   ILETHRLEUTYRLYSASPLEULYSPROVAL
5   LEUASPSERTYRVALPHEASNASPGLYSER
6   SERARGGLULEUMETASNLEUTHRGLYTHR
7   ILEPROVALPROTYRARGGLYASNTHRTYR
8   ASNILEPROILECYSLEUTRPLEULEUASP
9   THRTYRPROTYRASNPROPROILECYSPHE
10   VALLYSPROTHRSERSERMETTHRILELYS
11   THRGLYLYSHISVALASPALAASNGLYLYS
12   ILETYRLEUPROTYRLEUHISGLUTRPLYS
13   HISPROGLNSERASPLEULEUGLYLEUILE
14   GLNVALMETILEVALVALPHEGLYASPGLU
15   PROPROVALPHESERARGPRO

Samples:

sample_1: Tsg101_UEV, [U-99% 13C; U-99% 15N], 330 uM; sodium phosphate 50 mM; sodium chloride 50 mM; EDTA 0.1 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.1; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CA)NNHsample_1isotropicsample_conditions_1
3D HCANsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D (H)CACONsample_1isotropicsample_conditions_1
2D CONsample_1isotropicsample_conditions_1
2D CACOsample_1isotropicsample_conditions_1

Software:

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

TOPSPIN - collection

NMRPipe - processing

qMDD - processing

NMR spectrometers:

  • Bruker AVANCE III HD 600 MHz

Related Database Links:

UNP Q99816

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