Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16035
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Knowles, Timothy; McClelland, Darren; Rajesh, Sandya; Henderson, Ian; Overduin, Michael. "Secondary structure and (1)H, (13)C and (15)N backbone resonance assignments of BamC, a component of the outer membrane protein assembly machinery in Escherichia coli." Biomol. NMR Assignments 3, 203-206 (2009).
PubMed: 19888691
Assembly members:
BamC, polymer, 322 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: chemical synthesis
Data type | Count |
13C chemical shifts | 929 |
15N chemical shifts | 302 |
1H chemical shifts | 302 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | BamC | 1 |
Entity 1, BamC 322 residues - Formula weight is not available
This sequence represents the final processed E. coli BamC sequence lacking its N-terminal signal peptide and mutated (C26S) to remove its lipoprotein acylation site. The first three residues (HMG) are derived from the vector.
1 | HIS | MET | GLY | SER | SER | ASP | SER | ARG | TYR | LYS | ||||
2 | ARG | GLN | VAL | SER | GLY | ASP | GLU | ALA | TYR | LEU | ||||
3 | GLU | ALA | ALA | PRO | LEU | ALA | GLU | LEU | HIS | ALA | ||||
4 | PRO | ALA | GLY | MET | ILE | LEU | PRO | VAL | THR | SER | ||||
5 | GLY | ASP | TYR | ALA | ILE | PRO | VAL | THR | ASN | GLY | ||||
6 | SER | GLY | ALA | VAL | GLY | LYS | ALA | LEU | ASP | ILE | ||||
7 | ARG | PRO | PRO | ALA | GLN | PRO | LEU | ALA | LEU | VAL | ||||
8 | SER | GLY | ALA | ARG | THR | GLN | PHE | THR | GLY | ASP | ||||
9 | THR | ALA | SER | LEU | LEU | VAL | GLU | ASN | GLY | ARG | ||||
10 | GLY | ASN | THR | LEU | TRP | PRO | GLN | VAL | VAL | SER | ||||
11 | VAL | LEU | GLN | ALA | LYS | ASN | TYR | THR | ILE | THR | ||||
12 | GLN | ARG | ASP | ASP | ALA | GLY | GLN | THR | LEU | THR | ||||
13 | THR | ASP | TRP | VAL | GLN | TRP | ASN | ARG | LEU | ASP | ||||
14 | GLU | ASP | GLU | GLN | TYR | ARG | GLY | ARG | TYR | GLN | ||||
15 | ILE | SER | VAL | LYS | PRO | GLN | GLY | TYR | GLN | GLN | ||||
16 | ALA | VAL | THR | VAL | LYS | LEU | LEU | ASN | LEU | GLU | ||||
17 | GLN | ALA | GLY | LYS | PRO | VAL | ALA | ASP | ALA | ALA | ||||
18 | SER | MET | GLN | ARG | TYR | SER | THR | GLU | MET | MET | ||||
19 | ASN | VAL | ILE | SER | ALA | GLY | LEU | ASP | LYS | SER | ||||
20 | ALA | THR | ASP | ALA | ALA | ASN | ALA | ALA | GLN | ASN | ||||
21 | ARG | ALA | SER | THR | THR | MET | ASP | VAL | GLN | SER | ||||
22 | ALA | ALA | ASP | ASP | THR | GLY | LEU | PRO | MET | LEU | ||||
23 | VAL | VAL | ARG | GLY | PRO | PHE | ASN | VAL | VAL | TRP | ||||
24 | GLN | ARG | LEU | PRO | ALA | ALA | LEU | GLU | LYS | VAL | ||||
25 | GLY | MET | LYS | VAL | THR | ASP | SER | THR | ARG | SER | ||||
26 | GLN | GLY | ASN | MET | ALA | VAL | THR | TYR | LYS | PRO | ||||
27 | LEU | SER | ASP | SER | ASP | TRP | GLN | GLU | LEU | GLY | ||||
28 | ALA | SER | ASP | PRO | GLY | LEU | ALA | SER | GLY | ASP | ||||
29 | TYR | LYS | LEU | GLN | VAL | GLY | ASP | LEU | ASP | ASN | ||||
30 | ARG | SER | SER | LEU | GLN | PHE | ILE | ASP | PRO | LYS | ||||
31 | GLY | HIS | THR | LEU | THR | GLN | SER | GLN | ASN | ASP | ||||
32 | ALA | LEU | VAL | ALA | VAL | PHE | GLN | ALA | ALA | PHE | ||||
33 | SER | LYS |
sample_1: BamC, [U-13C; U-15N; U-2H], 1 mM; sodium phosphate 50 mM; potassium chloride 50 mM; sodium azide 0.02%
sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 303 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N TROSY HSQC | sample_1 | isotropic | sample_conditions_1 |
3D TROSY HNCA | sample_1 | isotropic | sample_conditions_1 |
3D TROSY HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D TROSY HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D TROSY HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
3D TROSY HNCO | sample_1 | isotropic | sample_conditions_1 |
3D TROSY HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
SPARKY v3.110, Goddard - chemical shift assignment, data analysis, peak picking
BMRB | 17521 |
PDB | |
DBJ | BAA16354 BAB36762 BAG78285 BAI26723 BAI31755 |
EMBL | CAA40661 CAP76938 CAQ32848 CAQ99368 CAR03928 |
GB | AAC75530 AAG57587 AAN44023 AAN81455 AAP17837 |
REF | NP_311366 NP_416972 NP_708316 WP_000968412 WP_001295468 |
SP | P0A903 P0A904 |
AlphaFold | P0A903 P0A904 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks