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 27381

Title: Backbone assignment of human TRIM25 PRYSPRY domain   PubMed: 29739942

Deposition date: 2018-01-23 Original release date: 2018-05-22

Authors: Haubrich, Kevin; Hennig, Janosch

Citation: Koliopoulos, Marios; Lethier, Mathilde; van der Veen, Annemarthe; Haubrich, Kevin; Hennig, Janosch; Kowalinski, Eva; Stevens, Rebecca; Martin, Stephen; Reis e Sousa, Caetano; Cusack, Stephen; Rittinger, Katrin. "Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition"  Nat. Commun. 9, 1820-1820 (2018).

Assembly members:
TRIM25_PRYSPRY, polymer, 194 residues, 22.2 Da.

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):
TRIM25_PRYSPRY: GPKVLETFLAKSRPELLEYY IKVILDYNTAHNKVALSECY TVASVAEMPQNYRPHPQRFT YCSQVLGLHCYKKGIHYWEV ELQKNNFCGVGICYGSMNRQ GPESRLGRNSASWCVEWFNT KISAWHNNVEKTLPSTKATR VGVLLNCDHGFVIFFAVADK VHLMYKFRVDFTEALYPAFW VFSAGATLSICSPK

Data sets:
Data typeCount
13C chemical shifts335
15N chemical shifts175
1H chemical shifts175

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PRYSPRY1

Entities:

Entity 1, PRYSPRY 194 residues - 22.2 Da.

GP artifact of precision protease cleavage. Native sequence corresonds to TRIM25 439-630

1   GLYPROLYSVALLEUGLUTHRPHELEUALA
2   LYSSERARGPROGLULEULEUGLUTYRTYR
3   ILELYSVALILELEUASPTYRASNTHRALA
4   HISASNLYSVALALALEUSERGLUCYSTYR
5   THRVALALASERVALALAGLUMETPROGLN
6   ASNTYRARGPROHISPROGLNARGPHETHR
7   TYRCYSSERGLNVALLEUGLYLEUHISCYS
8   TYRLYSLYSGLYILEHISTYRTRPGLUVAL
9   GLULEUGLNLYSASNASNPHECYSGLYVAL
10   GLYILECYSTYRGLYSERMETASNARGGLN
11   GLYPROGLUSERARGLEUGLYARGASNSER
12   ALASERTRPCYSVALGLUTRPPHEASNTHR
13   LYSILESERALATRPHISASNASNVALGLU
14   LYSTHRLEUPROSERTHRLYSALATHRARG
15   VALGLYVALLEULEUASNCYSASPHISGLY
16   PHEVALILEPHEPHEALAVALALAASPLYS
17   VALHISLEUMETTYRLYSPHEARGVALASP
18   PHETHRGLUALALEUTYRPROALAPHETRP
19   VALPHESERALAGLYALATHRLEUSERILE
20   CYSSERPROLYS

Samples:

sample_1: TRIM25 PRYSPRY, [U-99% 13C; U-99% 15N], 0.45 ± 0.05 mM; sodium phosphate 20 mM; sodium chloride 150 mM; TCEP 0.2 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 170 mM; pH: 6.5; pressure: 1 atm; temperature: 289 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

Cara v1.8.4, Keller and Wuthrich - chemical shift assignment, peak picking

NMRPipe v8.7, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN v2.1, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

UNP Q14258

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