Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51113
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Johnson, Courtney; Xu, Xiaoping; Holloway, Stephen; Libich, David. "The 1H, 15N and 13C resonance assignments of the low-complexity domain from the oncogenic fusion protein EWS-FLI1" Biomol. NMR Assignments 16, 67-73 (2022).
PubMed: 34994941
Assembly members:
entity_1, polymer, 94 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pAG8H-GB1
Entity Sequences (FASTA):
entity_1: TYPQVPGSYPMQPVTAPPSY
PPTSYSSTQPTSYDQSSYSQ
QNTYGQPSSYGQQSSYGQQS
SYGQQPPTSYPPQTGSYSQA
PSQYSQQSSSYGQQ
Data type | Count |
13C chemical shifts | 262 |
15N chemical shifts | 78 |
1H chemical shifts | 78 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | EWSR1 171-264 | 1 |
Entity 1, EWSR1 171-264 94 residues - Formula weight is not available
1 | THR | TYR | PRO | GLN | VAL | PRO | GLY | SER | TYR | PRO | ||||
2 | MET | GLN | PRO | VAL | THR | ALA | PRO | PRO | SER | TYR | ||||
3 | PRO | PRO | THR | SER | TYR | SER | SER | THR | GLN | PRO | ||||
4 | THR | SER | TYR | ASP | GLN | SER | SER | TYR | SER | GLN | ||||
5 | GLN | ASN | THR | TYR | GLY | GLN | PRO | SER | SER | TYR | ||||
6 | GLY | GLN | GLN | SER | SER | TYR | GLY | GLN | GLN | SER | ||||
7 | SER | TYR | GLY | GLN | GLN | PRO | PRO | THR | SER | TYR | ||||
8 | PRO | PRO | GLN | THR | GLY | SER | TYR | SER | GLN | ALA | ||||
9 | PRO | SER | GLN | TYR | SER | GLN | GLN | SER | SER | SER | ||||
10 | TYR | GLY | GLN | GLN |
sample_1: EWSR1 171-264, [U-100% 13C; U-100% 15N], 100 uM; MES 20 mM; PMSF 0.1 mM; EDTA 1 mM
sample_conditions_1: pH: 6.2; pressure: 1 atm; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
ANALYSIS - chemical shift assignment
TOPSPIN - collection
NMRPipe - processing
NMRDraw - processing
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks