BMRB Entry 6061
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6061
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the N-terminal 69 Amino Acid Residues of the ColE9 T1-61-DNase Fusion Protein PubMed: 15452437
Deposition date: 2004-01-06 Original release date: 2004-10-29
Authors: Tozawa, Kaeko; Macdonald, Colin; Collins, Emily; Penfold, Christopher; James, Richard; Kleanthous, Colin; Clayden, Nigel; Moore, Geoffrey
Citation: Macdonald, Colin; Tozawa, Kaeko; Collins, Emily; Penfold, Christopher; James, Richard; Kleanthous, Colin; Clayden, Nigel; Moore, Geoffrey. "Characterisation of a mobile protein-binding epitope in the translocation domain of colicin E9 " J. Biomol. NMR 30, 81-96 (2004).
Assembly members:
T1-61-E9DNase fusion protein, polymer, 202 residues, 21292 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pNP330
Entity Sequences (FASTA):
T1-61-E9DNase fusion protein: MSGGDGRGHNTGAHSTSGNI
NGGPTGIGVSGGASDGSGWS
SENNPWGGGSGSGIHWGGGS
GLVPRGSAMESKRNKPGKAT
GKGKPVGDKWLDDAGKDSGA
PIPDRIADKLRDKEFKSFDD
FRKAVWEEVSKDPELSKNLN
PSNKSSVSKGYSPFTPKNQQ
VGGRKVYELHHDKPISQGGE
VYDMDNIRVTTPKRHIDIHR
GK
- assigned_chemical_shifts
Data type | Count |
1H chemical shifts | 268 |
13C chemical shifts | 169 |
15N chemical shifts | 60 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | T1-61-DNase fusion protein | 1 |
Entities:
Entity 1, T1-61-DNase fusion protein 202 residues - 21292 Da.
1 | MET | SER | GLY | GLY | ASP | GLY | ARG | GLY | HIS | ASN | ||||
2 | THR | GLY | ALA | HIS | SER | THR | SER | GLY | ASN | ILE | ||||
3 | ASN | GLY | GLY | PRO | THR | GLY | ILE | GLY | VAL | SER | ||||
4 | GLY | GLY | ALA | SER | ASP | GLY | SER | GLY | TRP | SER | ||||
5 | SER | GLU | ASN | ASN | PRO | TRP | GLY | GLY | GLY | SER | ||||
6 | GLY | SER | GLY | ILE | HIS | TRP | GLY | GLY | GLY | SER | ||||
7 | GLY | LEU | VAL | PRO | ARG | GLY | SER | ALA | MET | GLU | ||||
8 | SER | LYS | ARG | ASN | LYS | PRO | GLY | LYS | ALA | THR | ||||
9 | GLY | LYS | GLY | LYS | PRO | VAL | GLY | ASP | LYS | TRP | ||||
10 | LEU | ASP | ASP | ALA | GLY | LYS | ASP | SER | GLY | ALA | ||||
11 | PRO | ILE | PRO | ASP | ARG | ILE | ALA | ASP | LYS | LEU | ||||
12 | ARG | ASP | LYS | GLU | PHE | LYS | SER | PHE | ASP | ASP | ||||
13 | PHE | ARG | LYS | ALA | VAL | TRP | GLU | GLU | VAL | SER | ||||
14 | LYS | ASP | PRO | GLU | LEU | SER | LYS | ASN | LEU | ASN | ||||
15 | PRO | SER | ASN | LYS | SER | SER | VAL | SER | LYS | GLY | ||||
16 | TYR | SER | PRO | PHE | THR | PRO | LYS | ASN | GLN | GLN | ||||
17 | VAL | GLY | GLY | ARG | LYS | VAL | TYR | GLU | LEU | HIS | ||||
18 | HIS | ASP | LYS | PRO | ILE | SER | GLN | GLY | GLY | GLU | ||||
19 | VAL | TYR | ASP | MET | ASP | ASN | ILE | ARG | VAL | THR | ||||
20 | THR | PRO | LYS | ARG | HIS | ILE | ASP | ILE | HIS | ARG | ||||
21 | GLY | LYS |
Samples:
sample-1: T1-61-E9DNase fusion protein, [U-15N], 1.0 mM
sample-2: T1-61-E9DNase fusion protein, [U-13C; U-15N], 0.8 mM
cond_1: pH: 6.3; temperature: 288 K
cond_2: pH: 6.05; temperature: 288 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
1H-15N HSQC | not available | not available | not available |
HNCA | not available | not available | not available |
HNCO | not available | not available | not available |
HNCACB | not available | not available | not available |
CBCA(CO)NH | not available | not available | not available |
(HCA)CO(CA)NH | not available | not available | not available |
HCCONH | not available | not available | not available |
C(CO)NH | not available | not available | not available |
HNN | not available | not available | not available |
Software:
XEASY -
NMR spectrometers:
- Varian INOVA 499.865 MHz
- Varian INOVA 599.162 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts