Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15019
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Citation: Oxenoid, Kirill; Kim, Hak Jun; Jacob, Jaison; Sonnichsen, Frank; Sanders, Chuck. "NMR assignments for a helical 40 kDa membrane protein" J. Am. Chem. Soc. 126, 5048-5049 (2004).
PubMed: 15099070
Assembly members:
DAGK, polymer, 122 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pSD005
Entity Sequences (FASTA):
DAGK: MANNTTGFTRIIKAAGYSWK
GLRAAWINEAAFRQEGVAVL
LAVVIACWLDVDAITRVLLI
SSVMLVMIVEILNSAIEAVV
DRIGSEYHELSGRAKDMGSA
AVLIAIIVAVITWCILLWSH
FG
Data type | Count |
13C chemical shifts | 320 |
15N chemical shifts | 109 |
1H chemical shifts | 109 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | DAGK monomer 1 | 1 |
2 | DAGK monomer 2 | 1 |
3 | DAGK monomer 3 | 1 |
Entity 1, DAGK monomer 1 122 residues - Formula weight is not available
1 | MET | ALA | ASN | ASN | THR | THR | GLY | PHE | THR | ARG | ||||
2 | ILE | ILE | LYS | ALA | ALA | GLY | TYR | SER | TRP | LYS | ||||
3 | GLY | LEU | ARG | ALA | ALA | TRP | ILE | ASN | GLU | ALA | ||||
4 | ALA | PHE | ARG | GLN | GLU | GLY | VAL | ALA | VAL | LEU | ||||
5 | LEU | ALA | VAL | VAL | ILE | ALA | CYS | TRP | LEU | ASP | ||||
6 | VAL | ASP | ALA | ILE | THR | ARG | VAL | LEU | LEU | ILE | ||||
7 | SER | SER | VAL | MET | LEU | VAL | MET | ILE | VAL | GLU | ||||
8 | ILE | LEU | ASN | SER | ALA | ILE | GLU | ALA | VAL | VAL | ||||
9 | ASP | ARG | ILE | GLY | SER | GLU | TYR | HIS | GLU | LEU | ||||
10 | SER | GLY | ARG | ALA | LYS | ASP | MET | GLY | SER | ALA | ||||
11 | ALA | VAL | LEU | ILE | ALA | ILE | ILE | VAL | ALA | VAL | ||||
12 | ILE | THR | TRP | CYS | ILE | LEU | LEU | TRP | SER | HIS | ||||
13 | PHE | GLY |
sample_1: DAGK, [U-13C; U-15N; U-2H], 3 mM
sample_conditions_1: pH: 6.5; temperature: 318 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
NMRPipe, F Delaglio, S Grzesiek, GW Vuister, G Zhu, J Pfeifer and A Bax - processing
NMRView, B Johnson, One Moon Scientific - chemical shift assignment
PDB | |
DBJ | BAB38448 BAE78044 BAG79858 BAI28303 BAI33480 |
EMBL | CAP78501 CAQ34391 CAR01021 CAR05676 CAR10862 |
GB | AAA24394 AAC43136 AAC77012 AAG59241 AAN45585 |
REF | NP_313052 NP_418466 NP_709878 WP_000002899 WP_000002905 |
SP | P0ABN1 P0ABN2 P0ABN3 P0ABN4 |
AlphaFold | P0ABN1 P0ABN2 P0ABN3 P0ABN4 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks