BMRB Entry 17371
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17371
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Title: Solution NMR structure of N-terminal Ubiquitin-like domain of FUBI, a ribosomal protein S30 precursor from Homo sapiens. NorthEast Structural Genomics consortium (NESG) target HR6166
Deposition date: 2010-12-20 Original release date: 2011-01-24
Authors: Lemak, Alexander; Yee, Adelinda; Houliston, Scott; Semesi, Antony; Doherty, Ryan; Dhe-Paganon, Sirano; Arrowsmith, Cheryl
Citation: Lemak, Alexander; Yee, Adelinda; Houliston, Scott; Doherty, Ryan; Semesi, Antony; Dhe-Paganon, Sirano; Arrowsmith, Cheryl. "Solution NMR structure of human Ubiquitin-like protein hs00113." Not known ., .-..
Assembly members:
hs00113, polymer, 93 residues, 7764.862 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):
hs00113: MGSSHHHHHHSSGLVPRGSM
QLFVRAQELHTFEVTGQETV
AQIKAHVASLEGIAPEDQVV
LLAGAPLEDEATLGQCGVEA
LTTLEVAGRMLGG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 305 |
| 15N chemical shifts | 72 |
| 1H chemical shifts | 514 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | hs00113 | 1 |
Entities:
Entity 1, hs00113 93 residues - 7764.862 Da.
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | MET | ||||
| 3 | GLN | LEU | PHE | VAL | ARG | ALA | GLN | GLU | LEU | HIS | ||||
| 4 | THR | PHE | GLU | VAL | THR | GLY | GLN | GLU | THR | VAL | ||||
| 5 | ALA | GLN | ILE | LYS | ALA | HIS | VAL | ALA | SER | LEU | ||||
| 6 | GLU | GLY | ILE | ALA | PRO | GLU | ASP | GLN | VAL | VAL | ||||
| 7 | LEU | LEU | ALA | GLY | ALA | PRO | LEU | GLU | ASP | GLU | ||||
| 8 | ALA | THR | LEU | GLY | GLN | CYS | GLY | VAL | GLU | ALA | ||||
| 9 | LEU | THR | THR | LEU | GLU | VAL | ALA | GLY | ARG | MET | ||||
| 10 | LEU | GLY | GLY |
Samples:
sample_1: hs00113, [U-13C; U-15N], 0.5 mM; mops 10 mM; sodium chloride 450 mM; ZnSO4 10 mM; DTT 10 mM; NaN3 0.01%; benzamidine 10 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 450 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment
FMC, Lemak,Steren,Llinas, Arrowsmith - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
TALOS, Cornilescu, Delaglio and Bax - data analysis
PSVS, Bhattacharya and Montelione - structure validation
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts