BMRB Entry 5604
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR5604
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Title: Solution structure of the N-terminal domain of ZntA in the apo- and Zn(II) forms PubMed: 12417201
Deposition date: 2002-11-28 Original release date: 2003-03-24
Authors: Banci, L.; Bertini, I.; Ciofi-Baffoni, S.; Finney, L.; Outten, C.; O'Halloran, T.
Citation: Banci, L.; Bertini, I.; Ciofi-Baffoni, S.; Finney, L.; Outten, C.; O'Halloran, T.. "A new-zinc protein coordination site in intracellular metal trafficking: solution structure of the apo and Zn(II) forms of ZntA (46-118)" J. Mol. Biol. 323, 883-897 (2002).
Assembly members:
p-type ATPase, polymer, 73 residues, Formula weight is not available
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
Entity Sequences (FASTA):
p-type ATPase: SGTRYSWKVSGMDCAACARK
VENAVRQLAGVNQVQVLFAT
EKLVVDADNDIRAQVESALQ
KAGYSLRDEQAAE
- assigned_chemical_shifts
Data type | Count |
1H chemical shifts | 406 |
15N chemical shifts | 72 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | P-type zinc atpase | 1 |
Entities:
Entity 1, P-type zinc atpase 73 residues - Formula weight is not available
1 | SER | GLY | THR | ARG | TYR | SER | TRP | LYS | VAL | SER | ||||
2 | GLY | MET | ASP | CYS | ALA | ALA | CYS | ALA | ARG | LYS | ||||
3 | VAL | GLU | ASN | ALA | VAL | ARG | GLN | LEU | ALA | GLY | ||||
4 | VAL | ASN | GLN | VAL | GLN | VAL | LEU | PHE | ALA | THR | ||||
5 | GLU | LYS | LEU | VAL | VAL | ASP | ALA | ASP | ASN | ASP | ||||
6 | ILE | ARG | ALA | GLN | VAL | GLU | SER | ALA | LEU | GLN | ||||
7 | LYS | ALA | GLY | TYR | SER | LEU | ARG | ASP | GLU | GLN | ||||
8 | ALA | ALA | GLU |
Samples:
sample_1: p-type ATPase, [U-15N], 1.5 mM; phosphate buffer 100 mM; H2O 90%; D2O 10%
sample_2: p-type ATPase 2 mM; phosphate buffer 100 mM; H2O 90%; D2O 10%
sample_cond_1: pH: 7; temperature: 298 K; ionic strength: 100 mM; pressure: 1 atm
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 15N-separated NOESY | not available | not available | sample_cond_1 |
HNHA | not available | not available | sample_cond_1 |
2D NOESY | not available | not available | sample_cond_1 |
2D TOCSY | not available | not available | sample_cond_1 |
Software:
XWINNMR v1.3 - collection, processing
DYANA v1.5 - structure solution
CORMA - iterative matrix relaxation
AMBER v5.0 - refinement
xeasy v3.2 - data analysis
NMR spectrometers:
- Bruker AVANCE 700 MHz
Related Database Links:
PDB | |
DBJ | BAB37741 BAE77824 BAG79261 BAI32897 BAJ45202 |
EMBL | CAQ90919 CAR00414 CAR15077 CAV00282 CBG36554 |
GB | AAB18444 AAC76494 AAG58578 AAN44946 AAP19236 |
REF | NP_290017 NP_312345 NP_417926 NP_709239 NP_839425 |
SP | P37617 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts