BMRB Entry 30528
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30528
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Title: Shuttle proteins complex
Deposition date: 2018-10-23 Original release date: 2019-08-30
Authors: Chen, X.; Walters, K.
Citation: Chen, X.; Walters, K.. "Protein complex of receptor and shuttle factor" . ., .-..
Assembly members:
entity_1, polymer, 111 residues, 11826.878 Da.
entity_2, polymer, 78 residues, 8764.189 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):
entity_1: MLGLGASDFEFGVDPSADPE
LALALRVSMEEQRQRQEEEA
RRAAAASAAEAGIATTGTED
SDDALLKMTISQQEFGRTGL
PDLSSMTEEEQIAYAMQMSL
QGAEFGQAESA
entity_2: APAEPKIIKVTVKTPKEKEE
FAVPENSSVQQFKEAISKRF
KSQTDQLVLIFAGKILKDQD
TLIQHGIHDGLTVHLVIK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 851 |
| 15N chemical shifts | 279 |
| 1H chemical shifts | 1924 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2, 1 | 2 |
| 3 | entity_2, 2 | 2 |
Entities:
Entity 1, entity_1 111 residues - 11826.878 Da.
| 1 | MET | LEU | GLY | LEU | GLY | ALA | SER | ASP | PHE | GLU | ||||
| 2 | PHE | GLY | VAL | ASP | PRO | SER | ALA | ASP | PRO | GLU | ||||
| 3 | LEU | ALA | LEU | ALA | LEU | ARG | VAL | SER | MET | GLU | ||||
| 4 | GLU | GLN | ARG | GLN | ARG | GLN | GLU | GLU | GLU | ALA | ||||
| 5 | ARG | ARG | ALA | ALA | ALA | ALA | SER | ALA | ALA | GLU | ||||
| 6 | ALA | GLY | ILE | ALA | THR | THR | GLY | THR | GLU | ASP | ||||
| 7 | SER | ASP | ASP | ALA | LEU | LEU | LYS | MET | THR | ILE | ||||
| 8 | SER | GLN | GLN | GLU | PHE | GLY | ARG | THR | GLY | LEU | ||||
| 9 | PRO | ASP | LEU | SER | SER | MET | THR | GLU | GLU | GLU | ||||
| 10 | GLN | ILE | ALA | TYR | ALA | MET | GLN | MET | SER | LEU | ||||
| 11 | GLN | GLY | ALA | GLU | PHE | GLY | GLN | ALA | GLU | SER | ||||
| 12 | ALA |
Entity 2, entity_2, 1 78 residues - 8764.189 Da.
| 1 | ALA | PRO | ALA | GLU | PRO | LYS | ILE | ILE | LYS | VAL | ||||
| 2 | THR | VAL | LYS | THR | PRO | LYS | GLU | LYS | GLU | GLU | ||||
| 3 | PHE | ALA | VAL | PRO | GLU | ASN | SER | SER | VAL | GLN | ||||
| 4 | GLN | PHE | LYS | GLU | ALA | ILE | SER | LYS | ARG | PHE | ||||
| 5 | LYS | SER | GLN | THR | ASP | GLN | LEU | VAL | LEU | ILE | ||||
| 6 | PHE | ALA | GLY | LYS | ILE | LEU | LYS | ASP | GLN | ASP | ||||
| 7 | THR | LEU | ILE | GLN | HIS | GLY | ILE | HIS | ASP | GLY | ||||
| 8 | LEU | THR | VAL | HIS | LEU | VAL | ILE | LYS |
Samples:
sample_1: hRpn10 196-306, [U-100% 15N], 0.6 mM; UBQLN2 UBL 1.38 mM; NaPO4 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.1%
sample_2: hRpn10 196-306, [U-100% 13C], 0.6 mM; UBQLN2 UBL 1.38 mM; NaPO4 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.1%
sample_3: hRpn10 196-306, [U-100% 15N; U-100% 2H], 0.6 mM; UBQLN2 UBL 1.38 mM; NaPO4 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.1%
sample_4: hRpn10 196-306 0.6 mM; UBQLN2 UBL, [U-100% 13C; U-100% 15N], 0.6 mM; NaPO4 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.1%
sample_5: hRpn10 196-306 0.6 mM; UBQLN2 UBL, [U-100% 13C; U-100% 15N], 0.6 mM; NaPO4 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.1%
sample_6: UBQLN2 UBL, [U-100% 13C; U-100% 15N], 0.6 mM; NaPO4 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.1%
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_5 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_4 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C half-filter NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_6 | isotropic | sample_conditions_1 |
| 3D 1H-13C half-filter NOESY | sample_5 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_5 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_5 | isotropic | sample_conditions_1 |
| 3D 1H-13C half-filter NOESY | sample_6 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_5 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_5 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation
TALOS, Cornilescu, Delaglio and Bax - data analysis
ProcheckNMR, Laskowski and MacArthur - data analysis
NMR spectrometers:
- Bruker Avance 850 MHz
- Bruker Avance 800 MHz
- Bruker Avance 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts