Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15207
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Citation: Boudet, Julien; Chouquet, Anne; Chahboune, Aicha; Giustini, Cecile; Joris, Bernard; Simorre, Jean-Pierre; Bougault, Catherine. "1H, 13C and 15N resonance assignments of YajG, an Escherichia coli protein of unknown structure and function" Biomol. NMR Assignments 1, 89-91 (2007).
PubMed: 19636835
Assembly members:
yajg, polymer, 182 residues, 19990 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: Escherichia Genus/species: coli coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET26b
Data type | Count |
13C chemical shifts | 750 |
15N chemical shifts | 184 |
1H chemical shifts | 1167 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | yajg | 1 |
Entity 1, yajg 182 residues - 19990 Da.
Residues 175-182 represent a non-native C-terminal histidine tag Signal sequence at the N-terminus of yajg from E. coli (first 18 residues of Swiss-Prot entry P0ADA6) have been deleted.
1 | ALA | LYS | PRO | PRO | THR | THR | ILE | GLU | VAL | SER | ||||
2 | PRO | THR | ILE | THR | LEU | PRO | GLN | GLN | ASP | PRO | ||||
3 | SER | LEU | MET | GLY | VAL | THR | VAL | SER | ILE | ASN | ||||
4 | GLY | ALA | ASP | GLN | ARG | THR | ASP | GLN | ALA | LEU | ||||
5 | ALA | LYS | VAL | THR | ARG | ASP | ASN | GLN | ILE | VAL | ||||
6 | THR | LEU | THR | ALA | SER | ARG | ASP | LEU | ARG | PHE | ||||
7 | LEU | LEU | GLN | GLU | VAL | LEU | GLU | LYS | GLN | MET | ||||
8 | THR | ALA | ARG | GLY | TYR | MET | VAL | GLY | PRO | ASN | ||||
9 | GLY | PRO | VAL | ASN | LEU | GLN | ILE | ILE | VAL | SER | ||||
10 | GLN | LEU | TYR | ALA | ASP | VAL | SER | GLN | GLY | ASN | ||||
11 | VAL | ARG | TYR | ASN | ILE | ALA | THR | LYS | ALA | ASP | ||||
12 | ILE | ALA | ILE | ILE | ALA | THR | ALA | GLN | ASN | GLY | ||||
13 | ASN | LYS | MET | THR | LYS | ASN | TYR | ARG | ALA | SER | ||||
14 | TYR | ASN | VAL | GLU | GLY | ALA | PHE | GLN | ALA | SER | ||||
15 | ASN | LYS | ASN | ILE | ALA | ASP | ALA | VAL | ASN | SER | ||||
16 | VAL | LEU | THR | ASP | THR | ILE | ALA | ASP | MET | SER | ||||
17 | GLN | ASP | THR | SER | ILE | HIS | GLU | PHE | ILE | LYS | ||||
18 | GLN | ASN | ALA | ARG | LEU | GLU | HIS | HIS | HIS | HIS | ||||
19 | HIS | HIS |
sample_1: yajg, [U-100% 13C; U-100% 15N; 80% 2H], 0.85 ± 0.1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.02%; H2O 95%; D2O 5%
sample_2: yajg, [U-98% 13C; U-98% 15N], 1 ± 0.2 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.02%; H2O 90%; D2O 10%
sample_3: yajg, [U-98% 13C; U-98% 15N], 0.8 ± 0.2 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.02%; D2O 100%
sample_4: yajg, [U-100% 13C; U-100% 15N; 80% 2H], 0.75 ± 0.1 mM; MES 50 mM; sodium chloride 100 mM; sodium azide 0.02%; D2O 5%; H2O 95%
sample_conditions_1: ionic strength: 175 mM; pH: 7.0; pressure: 1 atm; temperature: 310 K
sample_conditions_2: ionic strength: 150 mM; pH: 6.0; pressure: 1 atm; temperature: 310 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
3D H(C)CH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D (H)CCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
2D Methyl-selective HSQC | sample_2 | isotropic | sample_conditions_1 |
3D Methyl-selective-NOESY-HSQC | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_4 | isotropic | sample_conditions_2 |
2D 1H-15N HSQC | sample_4 | isotropic | sample_conditions_2 |
2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
HBCBCGCDHD | sample_3 | isotropic | sample_conditions_1 |
HBCBCGCDCEHE | sample_3 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView v5.2.2, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
VNMRJ v2.1, Varian - collection
DBJ | BAB33911 BAE76214 BAG75983 BAI23808 BAI29279 |
EMBL | CAP74968 CAQ30906 CAQ97309 CAR01777 CAR06667 |
GB | AAB28883 AAB40190 AAC73537 AAG54784 AAN42034 |
REF | NP_308515 NP_414968 NP_706327 WP_000473497 WP_000473498 |
SP | P0ADA5 P0ADA6 |
AlphaFold | P0ADA5 P0ADA6 |
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SPARKY: Backbone
or all simulated peaks