BMRB Entry 7318
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7318
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Title: Backbone 1HN, 15N, and 13C Chemical Shift Assignments for wt Im7* (* denotes his-tag) and its variants, Im7*L53AI54A and Im7*YY PubMed: 17188712
Deposition date: 2006-10-17 Original release date: 2007-05-04
Authors: Whittaker, Sara; Spence, Graham; Grossmann, Guenter; Radford, Sheena; Moore, Geoffrey
Citation: Whittaker, Sara; Spence, Graham; Grossmann, Guenter; Radford, Sheena; Moore, Geoffrey. "NMR analysis of the conformational properties of the trapped on-pathway folding intermediate of the bacterial immunity protein Im7." J. Mol. Biol. 366, 1001-1015 (2007).
Assembly members:
YY, polymer, 94 residues, Formula weight is not available
Natural source: Common Name: Escherichia coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
YY: MEHHHHHHELKNSISDYTEA
EFVQLLKEIEKENVAATDDV
LDVLLEHFVKITEHPDGGGG
GYYPSDNRDDSPEGIVKEIK
EWRAANGKPGFKQG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 202 |
| 15N chemical shifts | 68 |
| 1H chemical shifts | 101 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Monomer | 1 |
Entities:
Entity 1, Monomer 94 residues - Formula weight is not available
The sequence of YY contains an N-terminal His-tag. Residue numbering starts at residue 2 of wt Im7 (no his-tag). Compared with Im7*, the residues T51-I54 have been mutated to Gly.
| 1 | MET | GLU | HIS | HIS | HIS | HIS | HIS | HIS | GLU | LEU | ||||
| 2 | LYS | ASN | SER | ILE | SER | ASP | TYR | THR | GLU | ALA | ||||
| 3 | GLU | PHE | VAL | GLN | LEU | LEU | LYS | GLU | ILE | GLU | ||||
| 4 | LYS | GLU | ASN | VAL | ALA | ALA | THR | ASP | ASP | VAL | ||||
| 5 | LEU | ASP | VAL | LEU | LEU | GLU | HIS | PHE | VAL | LYS | ||||
| 6 | ILE | THR | GLU | HIS | PRO | ASP | GLY | GLY | GLY | GLY | ||||
| 7 | GLY | TYR | TYR | PRO | SER | ASP | ASN | ARG | ASP | ASP | ||||
| 8 | SER | PRO | GLU | GLY | ILE | VAL | LYS | GLU | ILE | LYS | ||||
| 9 | GLU | TRP | ARG | ALA | ALA | ASN | GLY | LYS | PRO | GLY | ||||
| 10 | PHE | LYS | GLN | GLY |
Samples:
sample_1: Im7*, [U-13C; U-15N], 1 ± 0.2 mM; potassium phosphate buffer 50 mM; sodium sulphate 400 mM; H2O 90%; D2O 10%
sample_2: Im7*, [U-99% 15N], 1 ± 0.2 mM; potassium phosphate buffer 50 mM; sodium sulphate 400 mM; H2O 90%; D2O 10%
conditions_1: pH: 7; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1H15N HSQC | not available | not available | conditions_1 |
| HNCO | Samples_1_and_3_and_5 | not available | conditions_1 |
| HNCA | Samples_3_and_5 | not available | conditions_1 |
| HNCOCA | Samples_3_and_5_again | not available | conditions_1 |
| CBCACONH | Samples_3_and_5_again2 | not available | conditions_1 |
| HNCACB | sample_1 | not available | conditions_1 |
| 1H-1H-15N NOESY-HSQC | not available | not available | conditions_1 |
Software:
No software information available
NMR spectrometers:
- Varian Inova 500 MHz
- Varian Inova 600 MHz
- Varian Inova 750 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts