BMRB Entry 26933
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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/BMR26933
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Title: Backbone assignment of unlinked NS2B-NS3 Protease of Zika Virus in complex with acetyl-lysine-arginine aldehyde PubMed: 28689970
Deposition date: 2016-11-04 Original release date: 2017-07-17
Authors: Li, Yan; Zhang, Zhenzhen; Phoo, Wint Wint; Loh, Ying Ru; Wang, Wei Ling; Chen, Ming Wei; Liu, Shuang; Hung, Alvin; Keller, Thomas H; Luo, Dahai; Kang, CongBao
Citation: Li, Yan; Zhang, Zhenzhen; Phoo, Wint Wint; Loh, Ying Ru; Wang, Weiling; Liu, Shuang; Chen, Ming Wei; Hung, Alvin; Keller, Thomas; Luo, Dahai; Kang, CongBao. "Structural Dynamics of Zika Virus NS2B-NS3 Protease Binding to Dipeptide Inhibitors" Structure 2126, 30186-30187 (2017).
Assembly members:
NS2B_fragment, polymer, 73 residues, Formula weight is not available
NS3_fragment, polymer, 178 residues, Formula weight is not available
entity_7HS, non-polymer, 328.411 Da.
Natural source: Common Name: Zika virus Taxonomy ID: 64320 Superkingdom: Viruses Kingdom: not available Genus/species: Zika virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b
Entity Sequences (FASTA):
NS2B_fragment: MGSSHHHHHHSSGLVPRGSH
MTGKSVDMYIERAGDITWEK
DAEVTGNSPRLDVALDESGD
FSLVEEDGPPMRE
NS3_fragment: GSGALWDVPAPKEVKKGETT
DGVYRVMTRKLLGSTQVGVG
VMQEGVFHTMWHVTKGAALR
SGEGRLDPYWGDVKQDLVSY
CGPWKLDAAWDGLSEVQLLA
VPPGERAKNIQTLPGIFKTK
DGDIGAVALDYPAGTSGSPI
LDKCGRVIGLYGNGVVIKNG
SYVSAITQGKREEETPVE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 592 |
| 15N chemical shifts | 191 |
| 1H chemical shifts | 191 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NS2B fragment (45-96) | 1 |
| 2 | NS3 fragment (1-177) | 2 |
| 3 | acetyl-lysine-arginine aldehyde | 3 |
Entities:
Entity 1, NS2B fragment (45-96) 73 residues - Formula weight is not available
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | THR | GLY | LYS | SER | VAL | ASP | MET | TYR | ILE | ||||
| 4 | GLU | ARG | ALA | GLY | ASP | ILE | THR | TRP | GLU | LYS | ||||
| 5 | ASP | ALA | GLU | VAL | THR | GLY | ASN | SER | PRO | ARG | ||||
| 6 | LEU | ASP | VAL | ALA | LEU | ASP | GLU | SER | GLY | ASP | ||||
| 7 | PHE | SER | LEU | VAL | GLU | GLU | ASP | GLY | PRO | PRO | ||||
| 8 | MET | ARG | GLU |
Entity 2, NS3 fragment (1-177) 178 residues - Formula weight is not available
| 1 | GLY | SER | GLY | ALA | LEU | TRP | ASP | VAL | PRO | ALA | ||||
| 2 | PRO | LYS | GLU | VAL | LYS | LYS | GLY | GLU | THR | THR | ||||
| 3 | ASP | GLY | VAL | TYR | ARG | VAL | MET | THR | ARG | LYS | ||||
| 4 | LEU | LEU | GLY | SER | THR | GLN | VAL | GLY | VAL | GLY | ||||
| 5 | VAL | MET | GLN | GLU | GLY | VAL | PHE | HIS | THR | MET | ||||
| 6 | TRP | HIS | VAL | THR | LYS | GLY | ALA | ALA | LEU | ARG | ||||
| 7 | SER | GLY | GLU | GLY | ARG | LEU | ASP | PRO | TYR | TRP | ||||
| 8 | GLY | ASP | VAL | LYS | GLN | ASP | LEU | VAL | SER | TYR | ||||
| 9 | CYS | GLY | PRO | TRP | LYS | LEU | ASP | ALA | ALA | TRP | ||||
| 10 | ASP | GLY | LEU | SER | GLU | VAL | GLN | LEU | LEU | ALA | ||||
| 11 | VAL | PRO | PRO | GLY | GLU | ARG | ALA | LYS | ASN | ILE | ||||
| 12 | GLN | THR | LEU | PRO | GLY | ILE | PHE | LYS | THR | LYS | ||||
| 13 | ASP | GLY | ASP | ILE | GLY | ALA | VAL | ALA | LEU | ASP | ||||
| 14 | TYR | PRO | ALA | GLY | THR | SER | GLY | SER | PRO | ILE | ||||
| 15 | LEU | ASP | LYS | CYS | GLY | ARG | VAL | ILE | GLY | LEU | ||||
| 16 | TYR | GLY | ASN | GLY | VAL | VAL | ILE | LYS | ASN | GLY | ||||
| 17 | SER | TYR | VAL | SER | ALA | ILE | THR | GLN | GLY | LYS | ||||
| 18 | ARG | GLU | GLU | GLU | THR | PRO | VAL | GLU |
Entity 3, acetyl-lysine-arginine aldehyde - C14 H28 N6 O3 - 328.411 Da.
| 1 | 7HS |
Samples:
sample_1: NS2B_fragment, [U-13C; U-15N; U-2H], 0.8 mM; NS3_fragment, [U-13C; U-15N; U-2H], 0.8 mM; HEPES 20 mM; sodium chloride 150 mM; DTT 1 mM
sample_conditions_1: ionic strength: 170 mM; pH: 7.3; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Bruker Biospin, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Johnson, One Moon Scientific, Keller and Wuthrich - chemical shift assignment, processing
NMR spectrometers:
- Bruker Avance 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts