Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25990
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Citation: Hosek, Tomas; Calcada, Eduardo; Nogueira, Marcela; Salvi, Michele; Pagani, Talita; Felli, Isabella; Pierattelli, Roberta. "Structural and Dynamic Characterization of the Molecular Hub Early Region 1A (E1A) from Human Adenovirus" Chemistry 22, 13010-13013 (2016).
PubMed: 27490777
Assembly members:
E1A-13S, polymer, 299 residues, Formula weight is not available
Natural source: Common Name: Human adenovirus 5 Taxonomy ID: 28285 Superkingdom: Viruses Kingdom: not available Genus/species: Mastadenovirus Human mastadenovirus C
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET42
Entity Sequences (FASTA):
E1A-13S: MRHIICHGGVITEEMAASLL
DQLIEEVLADNLPPPSHFEP
PTLHELYDLDVTAPEDPNEE
AVSQIFPESVMLAVQEGIDL
FTFPPAPGSPEPPHLSRQPE
QPEQRALGPVSMPNLVPEVI
DLTCHEAGFPPSDDEDEEGE
EFVLDYVGHPGHGCRSCHYH
RRNTGDPDIMCSLCYMRTCG
MFVYSPVSEPEPEPEPEPEP
ARPTRRPKLVPAILRRPTSP
VSRECNSSTDSCDSGPSNTP
PEIHPVVPLCPIKPVAVRVG
GRRQAVECIEDLLNEPGQPL
DLSCKRPRPLEHHHHHHHH
Data type | Count |
13C chemical shifts | 572 |
15N chemical shifts | 167 |
1H chemical shifts | 167 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | E1A-13S | 1 |
Entity 1, E1A-13S 299 residues - Formula weight is not available
1 | MET | ARG | HIS | ILE | ILE | CYS | HIS | GLY | GLY | VAL | ||||
2 | ILE | THR | GLU | GLU | MET | ALA | ALA | SER | LEU | LEU | ||||
3 | ASP | GLN | LEU | ILE | GLU | GLU | VAL | LEU | ALA | ASP | ||||
4 | ASN | LEU | PRO | PRO | PRO | SER | HIS | PHE | GLU | PRO | ||||
5 | PRO | THR | LEU | HIS | GLU | LEU | TYR | ASP | LEU | ASP | ||||
6 | VAL | THR | ALA | PRO | GLU | ASP | PRO | ASN | GLU | GLU | ||||
7 | ALA | VAL | SER | GLN | ILE | PHE | PRO | GLU | SER | VAL | ||||
8 | MET | LEU | ALA | VAL | GLN | GLU | GLY | ILE | ASP | LEU | ||||
9 | PHE | THR | PHE | PRO | PRO | ALA | PRO | GLY | SER | PRO | ||||
10 | GLU | PRO | PRO | HIS | LEU | SER | ARG | GLN | PRO | GLU | ||||
11 | GLN | PRO | GLU | GLN | ARG | ALA | LEU | GLY | PRO | VAL | ||||
12 | SER | MET | PRO | ASN | LEU | VAL | PRO | GLU | VAL | ILE | ||||
13 | ASP | LEU | THR | CYS | HIS | GLU | ALA | GLY | PHE | PRO | ||||
14 | PRO | SER | ASP | ASP | GLU | ASP | GLU | GLU | GLY | GLU | ||||
15 | GLU | PHE | VAL | LEU | ASP | TYR | VAL | GLY | HIS | PRO | ||||
16 | GLY | HIS | GLY | CYS | ARG | SER | CYS | HIS | TYR | HIS | ||||
17 | ARG | ARG | ASN | THR | GLY | ASP | PRO | ASP | ILE | MET | ||||
18 | CYS | SER | LEU | CYS | TYR | MET | ARG | THR | CYS | GLY | ||||
19 | MET | PHE | VAL | TYR | SER | PRO | VAL | SER | GLU | PRO | ||||
20 | GLU | PRO | GLU | PRO | GLU | PRO | GLU | PRO | GLU | PRO | ||||
21 | ALA | ARG | PRO | THR | ARG | ARG | PRO | LYS | LEU | VAL | ||||
22 | PRO | ALA | ILE | LEU | ARG | ARG | PRO | THR | SER | PRO | ||||
23 | VAL | SER | ARG | GLU | CYS | ASN | SER | SER | THR | ASP | ||||
24 | SER | CYS | ASP | SER | GLY | PRO | SER | ASN | THR | PRO | ||||
25 | PRO | GLU | ILE | HIS | PRO | VAL | VAL | PRO | LEU | CYS | ||||
26 | PRO | ILE | LYS | PRO | VAL | ALA | VAL | ARG | VAL | GLY | ||||
27 | GLY | ARG | ARG | GLN | ALA | VAL | GLU | CYS | ILE | GLU | ||||
28 | ASP | LEU | LEU | ASN | GLU | PRO | GLY | GLN | PRO | LEU | ||||
29 | ASP | LEU | SER | CYS | LYS | ARG | PRO | ARG | PRO | LEU | ||||
30 | GLU | HIS | HIS | HIS | HIS | HIS | HIS | HIS | HIS |
sample_1: E1A-13S, [U-99% 13C; U-99% 15N], 0.2 mM; HEPES 10 mM; potassium chloride 150 mM; DTT 10 mM; H2O 90%; D2O, [U-2H], 10%
sample_2: E1A-13S, [U-99% 13C; U-99% 15N], 0.2 mM; HEPES 10 mM; potassium chloride 150 mM; DTT 10 mM; H2O 90%; D2O, [U-2H], 10%
sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 278 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D CON-IPAP | sample_1 | isotropic | sample_conditions_1 |
3D HCBCACON-IPAP | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N BEST-TROSY | sample_2 | isotropic | sample_conditions_1 |
3D BEST-TROSY HNCO | sample_2 | isotropic | sample_conditions_1 |
3D BEST-TROSY HNCACO | sample_2 | isotropic | sample_conditions_1 |
3D BEST-TROSY HNCOCACB | sample_2 | isotropic | sample_conditions_1 |
3D BEST-TROSY HNCACB | sample_2 | isotropic | sample_conditions_1 |
3D BEST-TROSY HN(CA)NNH | sample_2 | isotropic | sample_conditions_1 |
3D TROSY HN(COCA)NNH | sample_2 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
TOPSPIN v1.3 and 2.1, Bruker Biospin - collection
CcpNMR, CCPN - chemical shift assignment, data analysis, peak picking
Download HSQC peak lists in one of the following formats:
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