BMRB Entry 30285
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30285
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Title: Solution-state NMR structural ensemble of human Tsg101 UEV in complex with tenatoprazole PubMed: 29123089
Deposition date: 2017-04-21 Original release date: 2017-11-10
Authors: Strickland, Madeleine; Ehrlich, Lorna; Watanabe, Susan; Khan, Mahfuz; Strub, Marie-Paule; Luan, Chi-Hao; Powell, Michael; Leis, Jonathan; Tjandra, Nico; Carter, Carol
Citation: Strickland, Madeleine; Ehrlich, Lorna; Watanabe, Susan; Khan, Mahfuz; Strub, Marie-Paule; Luan, Chi-Hao; Powell, Michael; Leis, Jonathan; Tjandra, Nico; Carter, Carol. "Tsg101 chaperone function revealed by HIV-1 assembly inhibitors." Nat. Commun. 8, 1391-1391 (2017).
Assembly members:
entity_1, polymer, 145 residues, 16559.207 Da.
entity_4N1, non-polymer, 331.413 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: GAVSESQLKKMVSKYKYRDL
TVRETVNVITLYKDLKPVLD
SYVFNDGSSRELMNLTGTIP
VPYRGNTYNIPICLWLLDTY
PYNPPICFVKPTSSMTIKTG
KHVDANGKIYLPYLHEWKHP
QSDLLGLIQVMIVVFGDEPP
VFSRP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 521 |
| 15N chemical shifts | 143 |
| 1H chemical shifts | 1078 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 145 residues - 16559.207 Da.
| 1 | GLY | ALA | VAL | SER | GLU | SER | GLN | LEU | LYS | LYS | ||||
| 2 | MET | VAL | SER | LYS | TYR | LYS | TYR | ARG | ASP | LEU | ||||
| 3 | THR | VAL | ARG | GLU | THR | VAL | ASN | VAL | ILE | THR | ||||
| 4 | LEU | TYR | LYS | ASP | LEU | LYS | PRO | VAL | LEU | ASP | ||||
| 5 | SER | TYR | VAL | PHE | ASN | ASP | GLY | SER | SER | ARG | ||||
| 6 | GLU | LEU | MET | ASN | LEU | THR | GLY | THR | ILE | PRO | ||||
| 7 | VAL | PRO | TYR | ARG | GLY | ASN | THR | TYR | ASN | ILE | ||||
| 8 | PRO | ILE | CYS | LEU | TRP | LEU | LEU | ASP | THR | TYR | ||||
| 9 | PRO | TYR | ASN | PRO | PRO | ILE | CYS | PHE | VAL | LYS | ||||
| 10 | PRO | THR | SER | SER | MET | THR | ILE | LYS | THR | GLY | ||||
| 11 | LYS | HIS | VAL | ASP | ALA | ASN | GLY | LYS | ILE | TYR | ||||
| 12 | LEU | PRO | TYR | LEU | HIS | GLU | TRP | LYS | HIS | PRO | ||||
| 13 | GLN | SER | ASP | LEU | LEU | GLY | LEU | ILE | GLN | VAL | ||||
| 14 | MET | ILE | VAL | VAL | PHE | GLY | ASP | GLU | PRO | PRO | ||||
| 15 | VAL | PHE | SER | ARG | PRO |
Entity 2, entity_2 - C16 H19 N4 O2 S - 331.413 Da.
| 1 | 4N1 |
Samples:
sample_2: Tenatoprazole 0.6 mM; Tsg101, [U-13C; U-15N], 0.6 mM; potassium phosphate 20 mM; sodium chloride 50 mM
sample_1: Tenatoprazole 0.6 mM; Tsg101, [U-98% 13C; U-98% 15N], 0.6 mM; potassium phosphate 20 mM; sodium chloride 50 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 5.8; pressure: 1 atm; temperature: 300 K
sample_conditions_2: ionic strength: 0.1 mM; pH: 5.8 pH*; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_2 |
| 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_2 |
| 3D 1H-13C-12C filtered NOESY aliphatic | sample_1 | isotropic | sample_conditions_2 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
Analysis v2.4.2, CCPN - chemical shift assignment, data analysis, peak picking
Gaussian v9, Gaussian, Inc. - geometry optimization
NMRDraw v8.2, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRPipe v8.2, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PSVS v1.5, Bhattacharya and Montelione - data analysis
TALOS-N v4.12, Yang Shen and Ad Bax - data analysis
TOPSPIN v3.0, Bruker Biospin - collection
X-PLOR NIH v2.37.7, Schwieters, Kuszewski, Tjandra and Clore - structure calculation
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
- Bruker Avance 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts