BMRB Entry 30043
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30043
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: NMR solution structure of Mayaro virus macro domain
Deposition date: 2016-03-10 Original release date: 2017-12-13
Authors: Melekis, E.; Tsika, A.; Bentrop, D.; Papageorgiou, N.; Coutard, B.; Spyroulias, G.
Citation: Melekis, E.; Tsika, A.; Bentrop, D.; Papageorgiou, N.; Coutard, B.; Spyroulias, G.; Melekis, E.; Tsika, A.; Lichiere, J.; Chasapis, C.; Margiolaki, I.; Papageorgiou, N.; Coutard, B.; Bentrop, D.; Spyroulias, G.; Makrynitsa, G.; Ntonti, D.; Marousis, K.; Tsika, A.; Lichiere, J.; Papageorgiou, N.; Coutard, B.; Bentrop, D.; Spyroulias, G.; Papageorgiou, N.; Watier, Y.; Saunders, L.; Coutard, B.; Lantez, V.; Gould, E.; Fitch, A.; Wright, J.; Canard, B.; Margiolaki, I.. "NMR solution structure of Mayaro virus macro domain" . ., .-..
Assembly members:
entity_1, polymer, 166 residues, 18147.494 Da.
Natural source: Common Name: MAYV Taxonomy ID: 374990 Superkingdom: Viruses Kingdom: not available Genus/species: Alphavirus Mayaro virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
entity_1: MAPAYTVKRADIATAIEDAV
VNAANHRGQVGDGVCRAVAR
KWPQAFRNAATPVGTAKTVK
CDETYIIHAVGPNFNNTSEA
EGDRDLAAAYRAVAAEINRL
SISSVAIPLLSTGIFSAGKD
RVHQSLSHLLAAMDTTEARV
TIYCRDKTWEQKIKTVLQNR
HHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 441 |
| 15N chemical shifts | 136 |
| 1H chemical shifts | 917 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 166 residues - 18147.494 Da.
| 1 | MET | ALA | PRO | ALA | TYR | THR | VAL | LYS | ARG | ALA | ||||
| 2 | ASP | ILE | ALA | THR | ALA | ILE | GLU | ASP | ALA | VAL | ||||
| 3 | VAL | ASN | ALA | ALA | ASN | HIS | ARG | GLY | GLN | VAL | ||||
| 4 | GLY | ASP | GLY | VAL | CYS | ARG | ALA | VAL | ALA | ARG | ||||
| 5 | LYS | TRP | PRO | GLN | ALA | PHE | ARG | ASN | ALA | ALA | ||||
| 6 | THR | PRO | VAL | GLY | THR | ALA | LYS | THR | VAL | LYS | ||||
| 7 | CYS | ASP | GLU | THR | TYR | ILE | ILE | HIS | ALA | VAL | ||||
| 8 | GLY | PRO | ASN | PHE | ASN | ASN | THR | SER | GLU | ALA | ||||
| 9 | GLU | GLY | ASP | ARG | ASP | LEU | ALA | ALA | ALA | TYR | ||||
| 10 | ARG | ALA | VAL | ALA | ALA | GLU | ILE | ASN | ARG | LEU | ||||
| 11 | SER | ILE | SER | SER | VAL | ALA | ILE | PRO | LEU | LEU | ||||
| 12 | SER | THR | GLY | ILE | PHE | SER | ALA | GLY | LYS | ASP | ||||
| 13 | ARG | VAL | HIS | GLN | SER | LEU | SER | HIS | LEU | LEU | ||||
| 14 | ALA | ALA | MET | ASP | THR | THR | GLU | ALA | ARG | VAL | ||||
| 15 | THR | ILE | TYR | CYS | ARG | ASP | LYS | THR | TRP | GLU | ||||
| 16 | GLN | LYS | ILE | LYS | THR | VAL | LEU | GLN | ASN | ARG | ||||
| 17 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: Mayaro virus' macro domain 0.4 mM
sample_2: Mayaro virus' macro domain, [U-99% 15N], 0.4 mM
sample_3: Mayaro virus' macro domain, [U-99% 13C; U-99% 15N], 0.4 mM
sample_4: Mayaro virus' macro domain, [U-15N]-Ala-Leu-Val, 0.4 mM
sample_5: Mayaro virus' macro domain, [U-14N]-Arg, 0.4 mM
sample_6: Mayaro virus' macro domain, [U-14N]-Asn-Cys, 0.4 mM
sample_7: Mayaro virus' macro domain, [U-100% 13C; U-100% 15N; U-80% 2H], 0.4 mM
sample_8: Mayaro virus' macro domain 0.5 mM
sample_conditions_1: ionic strength: 20 mM; pH: 7; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 20 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_5 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_7 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_2 |
| 3D HBHA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC TROSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_3 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.3, Bruker Biospin - collection, processing
TOPSPIN v3.2, Bruker Biospin - collection, processing
CARA v1.5.5, Keller and Wuthrich - chemical shift assignment
XEASY, Bartels et al. - peak picking
DYANA, Guntert, Braun and Wuthrich - structure calculation
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
AMBER, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement
NMR spectrometers:
- Bruker Bruker Avance 600 MHz
- Bruker Bruker Avance III High-Definition four-channel 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts