Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18392
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Citation: Venditti, Vincenzo; Clore, G. Marius. "Conformational Selection and Substrate Binding Regulate the Monomer/Dimer Equilibrium of the C-terminal domain of Escherichia coli Enzyme I." J. Biol. Chem. 287, 26989-26998 (2012).
PubMed: 22722931
Assembly members:
EIC, polymer, 316 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: pET11a
Data type | Count |
13C chemical shifts | 810 |
15N chemical shifts | 266 |
1H chemical shifts | 266 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | EIC subunit 1 | 1 |
2 | EIC subunit 2 | 1 |
Entity 1, EIC subunit 1 316 residues - Formula weight is not available
1 | MET | ALA | ILE | THR | LEU | ASP | GLY | HIS | GLN | VAL | ||||
2 | GLU | VAL | CYS | ALA | ASN | ILE | GLY | THR | VAL | ARG | ||||
3 | ASP | VAL | GLU | GLY | ALA | GLU | ARG | ASN | GLY | ALA | ||||
4 | GLU | GLY | VAL | GLY | LEU | TYR | ARG | THR | GLU | PHE | ||||
5 | LEU | PHE | MET | ASP | ARG | ASP | ALA | LEU | PRO | THR | ||||
6 | GLU | GLU | GLU | GLN | PHE | ALA | ALA | TYR | LYS | ALA | ||||
7 | VAL | ALA | GLU | ALA | CYS | GLY | SER | GLN | ALA | VAL | ||||
8 | ILE | VAL | ARG | THR | MET | ASP | ILE | GLY | GLY | ASP | ||||
9 | LYS | GLU | LEU | PRO | TYR | MET | ASN | PHE | PRO | LYS | ||||
10 | GLU | GLU | ASN | PRO | PHE | LEU | GLY | TRP | ARG | ALA | ||||
11 | ILE | ARG | ILE | ALA | MET | ASP | ARG | LYS | GLU | ILE | ||||
12 | LEU | ARG | ASP | GLN | LEU | ARG | ALA | ILE | LEU | ARG | ||||
13 | ALA | SER | ALA | PHE | GLY | LYS | LEU | ARG | ILE | MET | ||||
14 | PHE | PRO | MET | ILE | ILE | SER | VAL | GLU | GLU | VAL | ||||
15 | ARG | ALA | LEU | ARG | LYS | GLU | ILE | GLU | ILE | TYR | ||||
16 | LYS | GLN | GLU | LEU | ARG | ASP | GLU | GLY | LYS | ALA | ||||
17 | PHE | ASP | GLU | SER | ILE | GLU | ILE | GLY | VAL | MET | ||||
18 | VAL | GLU | THR | PRO | ALA | ALA | ALA | THR | ILE | ALA | ||||
19 | ARG | HIS | LEU | ALA | LYS | GLU | VAL | ASP | PHE | PHE | ||||
20 | SER | ILE | GLY | THR | ASN | ASP | LEU | THR | GLN | TYR | ||||
21 | THR | LEU | ALA | VAL | ASP | ARG | GLY | ASN | ASP | MET | ||||
22 | ILE | SER | HIS | LEU | TYR | GLN | PRO | MET | SER | PRO | ||||
23 | SER | VAL | LEU | ASN | LEU | ILE | LYS | GLN | VAL | ILE | ||||
24 | ASP | ALA | SER | HIS | ALA | GLU | GLY | LYS | TRP | THR | ||||
25 | GLY | MET | CYS | GLY | GLU | LEU | ALA | GLY | ASP | GLU | ||||
26 | ARG | ALA | THR | LEU | LEU | LEU | LEU | GLY | MET | GLY | ||||
27 | LEU | ASP | GLU | PHE | SER | MET | SER | ALA | ILE | SER | ||||
28 | ILE | PRO | ARG | ILE | LYS | LYS | ILE | ILE | ARG | ASN | ||||
29 | THR | ASN | PHE | GLU | ASP | ALA | LYS | VAL | LEU | ALA | ||||
30 | GLU | GLN | ALA | LEU | ALA | GLN | PRO | THR | THR | ASP | ||||
31 | GLU | LEU | MET | THR | LEU | VAL | ASN | LYS | PHE | ILE | ||||
32 | GLU | GLU | LYS | THR | ILE | CYS |
BMRB | 25731 |
PDB | 2KX9 2L5H 2N5T 2XDF |
DBJ | BAA16290 BAB36711 BAG78231 BAH64557 BAI26669 |
EMBL | CAP76888 CAQ32794 CAQ88296 CAQ99314 CAR03878 |
GB | AAA24385 AAA24441 AAA27060 AAC75469 AAG57535 |
REF | NP_311315 NP_416911 NP_461367 NP_708271 WP_000112669 |
SP | P08839 P0A249 P0A250 |
AlphaFold | P08839 P0A249 P0A250 |
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