BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 51351

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51351

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Title: 1H, 13C and 15N resonance assignments of TSR3 domain of human Thrombospondin-1   PubMed: 35597280

Deposition date: 2022-03-07 Original release date: 2022-05-27

Authors: Eletsky, Alexander; Berardinelli, Steven; Ito, Atsuko; Takeuchi, Megumi; Haltiwanger, Robert

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).

Assembly members:
entity_1, polymer, 75 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   Vector: pET20b+

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

Data sets:
Data typeCount
13C chemical shifts273
15N chemical shifts74
1H chemical shifts429

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TSR31

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

Samples:

sample_1: TSR3, [U-13C; U-15N], 720 uM; sodium phosphate 20 mM; sodium chloride 100 mM; DSS 4 uM; sodium azide 0.02%

sample_2: TSR3, [U-13C; U-15N], 360 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
3D 1H-15N 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

AutoAssign - chemical shift assignment

NMR spectrometers:

  • Agilent DD2 800 MHz
  • Agilent DD2 900 MHz
  • Bruker AVANCE NEO 900 MHz
  • Varian VNMRS 600 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 shifts
SPARKY: Backbone or all simulated shifts