BMRB Entry 5595
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5595
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Title: Letter to the Editor: 1H, 13C, 15N backbone resonance assignments of apo-NosL, a novel 18.5 kDa copper(I) binding protein from the nitrous oxide reductase gene cluster of Achromobacter cycloclastes PubMed: 15014237
Deposition date: 2002-11-21 Original release date: 2004-03-15
Authors: Taubner, Lara; McGuirl, Michele; Dooley, David; Copie, Valerie
Citation: Taubner, Lara; McGuirl, Michele; Dooley, David; Copie, Valerie. "Letter to the Editor: 1H, 13C, 15N backbone and sidechain resonance assignments of apo-NosL, a novel copper(I) binding protein from the nitrous oxide reductase gene cluster of Achromobacter cycloclastes" J. Biomol. NMR 29, 211-212 (2004).
Assembly members:
NosL, polymer, 175 residues, 18538 Da.
Natural source: Common Name: Denitrifying bacteria Taxonomy ID: 223 Superkingdom: Eubacteria Kingdom: not available Genus/species: Achromobacter cycloclastes
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
NosL: MDKEDVAQSIVPQDMTPETL
GHYCQMNLLEHPGPKAQIFL
EGSPAPLFFSQVRDAIAYAR
GPEQIAPILVIYVNDMGAAG
ATWDQPGDGNWIAADKAFYV
VGSARRGGMGAPEAVPFSSR
DEAAAFVLAEGGQVLALADI
TDAMVLTPVETGSEPRADDE
DYLGRLRALPHPAGG
- assigned_chemical_shifts
Data type | Count |
1H chemical shifts | 846 |
13C chemical shifts | 596 |
15N chemical shifts | 148 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | NosL monomer | 1 |
Entities:
Entity 1, NosL monomer 175 residues - 18538 Da.
1 | MET | ASP | LYS | GLU | ASP | VAL | ALA | GLN | SER | ILE | ||||
2 | VAL | PRO | GLN | ASP | MET | THR | PRO | GLU | THR | LEU | ||||
3 | GLY | HIS | TYR | CYS | GLN | MET | ASN | LEU | LEU | GLU | ||||
4 | HIS | PRO | GLY | PRO | LYS | ALA | GLN | ILE | PHE | LEU | ||||
5 | GLU | GLY | SER | PRO | ALA | PRO | LEU | PHE | PHE | SER | ||||
6 | GLN | VAL | ARG | ASP | ALA | ILE | ALA | TYR | ALA | ARG | ||||
7 | GLY | PRO | GLU | GLN | ILE | ALA | PRO | ILE | LEU | VAL | ||||
8 | ILE | TYR | VAL | ASN | ASP | MET | GLY | ALA | ALA | GLY | ||||
9 | ALA | THR | TRP | ASP | GLN | PRO | GLY | ASP | GLY | ASN | ||||
10 | TRP | ILE | ALA | ALA | ASP | LYS | ALA | PHE | TYR | VAL | ||||
11 | VAL | GLY | SER | ALA | ARG | ARG | GLY | GLY | MET | GLY | ||||
12 | ALA | PRO | GLU | ALA | VAL | PRO | PHE | SER | SER | ARG | ||||
13 | ASP | GLU | ALA | ALA | ALA | PHE | VAL | LEU | ALA | GLU | ||||
14 | GLY | GLY | GLN | VAL | LEU | ALA | LEU | ALA | ASP | ILE | ||||
15 | THR | ASP | ALA | MET | VAL | LEU | THR | PRO | VAL | GLU | ||||
16 | THR | GLY | SER | GLU | PRO | ARG | ALA | ASP | ASP | GLU | ||||
17 | ASP | TYR | LEU | GLY | ARG | LEU | ARG | ALA | LEU | PRO | ||||
18 | HIS | PRO | ALA | GLY | GLY |
Samples:
15N_13C_sample: NosL, [U-15N; U-13C], 1.0 mM; DTT, [U-2D], 1.0 mM; EDTA 1.0 mM; D2O 10%; sodium phosphate 100 mM
15N_13C_NosL_cond: pH*: 6.5; temperature: 303 K; ionic strength: 0.1 M
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
15N HSQC | not available | not available | not available |
HNCACB | not available | not available | not available |
CBCA(CO)NH | not available | not available | not available |
CCONH | not available | not available | not available |
HCCONH | not available | not available | not available |
HBHACONH | not available | not available | not available |
HNCA | not available | not available | not available |
HNCO | not available | not available | not available |
15N-TOCSY | not available | not available | not available |
15N-NOESY | not available | not available | not available |
HCCH-TOCSY | not available | not available | not available |
Software:
NMRPipe - processing, peak picking, peak tables
PIPP - processing, peak picking, peak tables
XWINNMR v3.1 - processing
NMR spectrometers:
- BRUKER DRX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts