BMRB Entry 51356

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51356

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
1H, 13C and 15N resonance assignments of fucosylated TSR3 domain of human Thrombospondin-1
Deposition date:
2022-03-09
Original release date:
2022-05-27
Authors:
Eletsky, Alexander; Berardinelli, Steven; Ito, Atsuko; Takeuchi, Megumi; Haltiwanger, Robert
Citation:

Citation: Berardinelli, Steven; Eletsky, Alexander; Valero-Gonzales, Jessika; Ito, Atsuko; Manjunath, Rajashri; Hurtado-Gurerro, Ramon; Prestegard, James; Woods, Robert; Haltiwanger, Robert. "O-Fucosylation stabilizes the TSR3 motif in Thrombospondin-1 by interacting with nearby amino acids and protecting a disulfide bond"  J. Biol. Chem. 298, 102047-102047 (2022).
PubMed: 35597280

Assembly members:

Assembly members:
entity_1, polymer, 75 residues, Formula weight is not available
entity_FUC, non-polymer, 164.156 Da.

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: pET20b+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MDIGINSDPINGGWGPWSPW DICSVTCGGGVQKRSRLCNN PAPQFGGKDCVGDVTENQIC NKQDCPILEHHHHHH

Data sets:
Data typeCount
13C chemical shifts278
15N chemical shifts74
1H chemical shifts435

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TSR31
2fucose2

Entities:

Entity 1, TSR3 75 residues - Formula weight is not available

Residues 9-67 correspond to segment 490-548 of the native thrombospondin-1. Residues 1-8 and 68-75 represent non-native expression and purification tags. Residue 42 represents a naturally occuring sequence variant p.Thr523Ala.

1   METASPILEGLYILEASNSERASPPROILE
2   ASNGLYGLYTRPGLYPROTRPSERPROTRP
3   ASPILECYSSERVALTHRCYSGLYGLYGLY
4   VALGLNLYSARGSERARGLEUCYSASNASN
5   PROALAPROGLNPHEGLYGLYLYSASPCYS
6   VALGLYASPVALTHRGLUASNGLNILECYS
7   ASNLYSGLNASPCYSPROILELEUGLUHIS
8   HISHISHISHISHIS

Entity 2, fucose - C6 H12 O5 - 164.156 Da.

1   FUC

Samples:

sample_1: TSR3, [U-13C; U-15N], 260 uM; Fuc, [U-13C], 260 uM; sodium phosphate 20 mM; sodium chloride 100 mM; DSS 4 uM; sodium azide 0.02%

sample_2: TSR3, [U-13C; U-15N], 240 uM; Fuc 240 uM; sodium phosphate 20 mM; sodium chloride 100 mM; DSS 4 uM; sodium azide 0.02%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298.1 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C CT-HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C CT-HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D (HACA)CONHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D (H)CCH-COSY aliphaticsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSY aliphaticsample_1isotropicsample_conditions_1
3D (H)CCH-COSY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N,13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C CT-HSQC aliphaticsample_2isotropicsample_conditions_1

Software:

TOPSPIN - collection, processing

VNMRj - collection

NMRPipe - processing

istHMS - processing

CARA - chemical shift assignment

NMR spectrometers:

  • Agilent DD2 800 MHz
  • Agilent DD2 900 MHz
  • Bruker AVANCE NEO 900 MHz
  • Varian VNMRS 600 MHz

Related Database Links:

UNP P07996
AlphaFold Q59E99

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