BMRB Entry 6373
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6373
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Title: 1H, 13C and 15N backbone resonance assignments of LexA catalytic domain with the L89P/Q92W/D150H/E152A/K156A mutations PubMed: 15929009
Deposition date: 2004-10-29 Original release date: 2005-06-03
Authors: Okon, Mark; Pfuetzner, Richard; Vockovic, Marija; Little, John; Strynadka, Natalie; McIntosh, Lawrence
Citation: Okon, Mark; Pfuetzner, Richard; Vockovic, Marija; Little, John; Strynadka, Natalie; McIntosh, Lawrence. "Letter to the Editor: Backbone chemical shift assignments of the LexA catalytic domain in its active conformation." J. Biomol. NMR 31, 371-372 (2005).
Assembly members:
catalytic domain of LexA L89P/Q92W/D150H/E152A/K156A mutant, polymer, 135 residues, 14850 Da.
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: Bacteria Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
catalytic domain of LexA L89P/Q92W/D150H/E152A/K156A mutant: LLQEEEEGLPLVGRVAAGEP
LPAQWHIEGHYQVDPSLFKP
NADFLLRVSGMSMKDIGIMD
GDLLAVHKTQDVRNGQVVVA
RIHDAVTVARLKKQGNKVEL
LPENSEFKPIVVDLRQQSFT
IEGLAVGVIRNGDWL
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 377 |
15N chemical shifts | 125 |
1H chemical shifts | 125 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | catalytic domain of LexA L89P/Q92W/D150H/E152A/K156A mutant, chain 1 | 1 |
2 | catalytic domain of LexA L89P/Q92W/D150H/E152A/K156A mutant, chain 2 | 1 |
Entities:
Entity 1, catalytic domain of LexA L89P/Q92W/D150H/E152A/K156A mutant, chain 1 135 residues - 14850 Da.
1 | LEU | LEU | GLN | GLU | GLU | GLU | GLU | GLY | LEU | PRO | ||||
2 | LEU | VAL | GLY | ARG | VAL | ALA | ALA | GLY | GLU | PRO | ||||
3 | LEU | PRO | ALA | GLN | TRP | HIS | ILE | GLU | GLY | HIS | ||||
4 | TYR | GLN | VAL | ASP | PRO | SER | LEU | PHE | LYS | PRO | ||||
5 | ASN | ALA | ASP | PHE | LEU | LEU | ARG | VAL | SER | GLY | ||||
6 | MET | SER | MET | LYS | ASP | ILE | GLY | ILE | MET | ASP | ||||
7 | GLY | ASP | LEU | LEU | ALA | VAL | HIS | LYS | THR | GLN | ||||
8 | ASP | VAL | ARG | ASN | GLY | GLN | VAL | VAL | VAL | ALA | ||||
9 | ARG | ILE | HIS | ASP | ALA | VAL | THR | VAL | ALA | ARG | ||||
10 | LEU | LYS | LYS | GLN | GLY | ASN | LYS | VAL | GLU | LEU | ||||
11 | LEU | PRO | GLU | ASN | SER | GLU | PHE | LYS | PRO | ILE | ||||
12 | VAL | VAL | ASP | LEU | ARG | GLN | GLN | SER | PHE | THR | ||||
13 | ILE | GLU | GLY | LEU | ALA | VAL | GLY | VAL | ILE | ARG | ||||
14 | ASN | GLY | ASP | TRP | LEU |
Samples:
sample_1: catalytic domain of LexA L89P/Q92W/D150H/E152A/K156A mutant, [U-13C; U-15N], 1 mM; Phosphate buffer 20 mM
sample_conditions: pH: 7.0; temperature: 303 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
1H15N HSQC TROSY | not available | not available | not available |
HNCA TROSY | not available | not available | not available |
HNCACB | not available | not available | not available |
(HB)CBCA(CO)NH | not available | not available | not available |
HNCO TROSY | not available | not available | not available |
15N-edited NOESY | not available | not available | not available |
Software:
VNMR v6.1C, VARIAN -
NMR spectrometers:
- VARIAN UNITY-INOVA 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts