BMRB Entry 26312
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26312
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Title: Ufm1 PubMed: 16527251
Deposition date: 2021-08-15 Original release date: 2021-08-20
Authors: Sasakawa, Hiroaki; Kato, Koichi
Citation: Sasakawa, Hiroaki; Sakata, Eri; Yamaguchi, Yoshiki; Komatsu, Masaaki; Tatsumi, Kanako; Kominami, Eiki; Tanaka, Keiji; Kato, Koichi. "Solution structure and dynamics of Ufm1, a ubiquitin-fold modifier 1." Biochem. Biophys. Res. Commun. 343, 21-26 (2006).
Assembly members:
Ufm1, polymer, 90 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: pGEX6P-1
Entity Sequences (FASTA):
Ufm1: GPLGSMSKVSFKITLTSDPR
LPYKVLSVPESTPFTAVLKF
AAEEFKVPAATSAIITNDGI
GINPAQTAGNVFLKHGSELR
IIPRDRVGSC
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 235 |
| 15N chemical shifts | 81 |
| 1H chemical shifts | 463 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Ufm1 | 1 |
Entities:
Entity 1, Ufm1 90 residues - Formula weight is not available
| 1 | GLY | PRO | LEU | GLY | SER | MET | SER | LYS | VAL | SER | |
| 2 | PHE | LYS | ILE | THR | LEU | THR | SER | ASP | PRO | ARG | |
| 3 | LEU | PRO | TYR | LYS | VAL | LEU | SER | VAL | PRO | GLU | |
| 4 | SER | THR | PRO | PHE | THR | ALA | VAL | LEU | LYS | PHE | |
| 5 | ALA | ALA | GLU | GLU | PHE | LYS | VAL | PRO | ALA | ALA | |
| 6 | THR | SER | ALA | ILE | ILE | THR | ASN | ASP | GLY | ILE | |
| 7 | GLY | ILE | ASN | PRO | ALA | GLN | THR | ALA | GLY | ASN | |
| 8 | VAL | PHE | LEU | LYS | HIS | GLY | SER | GLU | LEU | ARG | |
| 9 | ILE | ILE | PRO | ARG | ASP | ARG | VAL | GLY | SER | CYS |
Samples:
sample_1: Ufm1, [U-13C; U-15N], 0.2 mM; sodium phosphate 10 mM; sodium chloride 100 mM; H2O 90%; D2O, [U-2H], 10%
sample_conditions_1: ionic strength: 100 mM; pH: 6.0; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 15N-edited TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe - processing
xwinnmr - processing
NMR spectrometers:
- JEOL ECA 920 MHz
- Bruker Avance 600 MHz
- Bruker DMX 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts