BMRB Entry 50310
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50310
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Title: Backbone 1H, and 15N chemical shift Assignments for the ligand-free GlnBP PubMed: 35446849
Deposition date: 2020-06-08 Original release date: 2022-05-09
Authors: Qin, Peiwu; Yu, Dongmei; Chen, Qun
Citation: Chen, Qun; Li, Fang; Zuo, Xiaobing; Chen, Jin; Qin, Peiwu; Wang, Chuhui; Xu, Jin; Yang, Danyu; Xing, Baogang; Liu, Ying; Jia, Peng; Li, Linling; Yang, Chengming; Yu, Dongmei. "Reversible domain closure modulates GlnBP ligand binding affinity" PLoS One 17, e0263102-e0263102 (2022).
Assembly members:
entity_1, polymer, 248 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
Entity Sequences (FASTA):
entity_1: MKSVLKVSLAALTLAFAVSS
HAADKKLVVATDTAFVPFEF
KQGDKYVGFDVDLWAAIAKE
LKLDYELKPMDFSGIIPALQ
TKNVDLALAGITITDERKKA
IDFSDGYYKSGLLVMVKANN
NDVKSVKDLDGKVVAVKSGT
GSVDYAKANIKTKDKRQFPN
IDNAYMELGTNRADAVLHDT
PNILYFIKTAGNGQFKAVGD
SLEAQQYGIAFPKGSDEQRD
KVNGALKTLRENGTYNEIYK
KWFGTEPK
- assigned_chemical_shifts
Data type | Count |
15N chemical shifts | 151 |
1H chemical shifts | 151 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | GlnBP | 1 |
Entities:
Entity 1, GlnBP 248 residues - Formula weight is not available
1 | MET | LYS | SER | VAL | LEU | LYS | VAL | SER | LEU | ALA | ||||
2 | ALA | LEU | THR | LEU | ALA | PHE | ALA | VAL | SER | SER | ||||
3 | HIS | ALA | ALA | ASP | LYS | LYS | LEU | VAL | VAL | ALA | ||||
4 | THR | ASP | THR | ALA | PHE | VAL | PRO | PHE | GLU | PHE | ||||
5 | LYS | GLN | GLY | ASP | LYS | TYR | VAL | GLY | PHE | ASP | ||||
6 | VAL | ASP | LEU | TRP | ALA | ALA | ILE | ALA | LYS | GLU | ||||
7 | LEU | LYS | LEU | ASP | TYR | GLU | LEU | LYS | PRO | MET | ||||
8 | ASP | PHE | SER | GLY | ILE | ILE | PRO | ALA | LEU | GLN | ||||
9 | THR | LYS | ASN | VAL | ASP | LEU | ALA | LEU | ALA | GLY | ||||
10 | ILE | THR | ILE | THR | ASP | GLU | ARG | LYS | LYS | ALA | ||||
11 | ILE | ASP | PHE | SER | ASP | GLY | TYR | TYR | LYS | SER | ||||
12 | GLY | LEU | LEU | VAL | MET | VAL | LYS | ALA | ASN | ASN | ||||
13 | ASN | ASP | VAL | LYS | SER | VAL | LYS | ASP | LEU | ASP | ||||
14 | GLY | LYS | VAL | VAL | ALA | VAL | LYS | SER | GLY | THR | ||||
15 | GLY | SER | VAL | ASP | TYR | ALA | LYS | ALA | ASN | ILE | ||||
16 | LYS | THR | LYS | ASP | LYS | ARG | GLN | PHE | PRO | ASN | ||||
17 | ILE | ASP | ASN | ALA | TYR | MET | GLU | LEU | GLY | THR | ||||
18 | ASN | ARG | ALA | ASP | ALA | VAL | LEU | HIS | ASP | THR | ||||
19 | PRO | ASN | ILE | LEU | TYR | PHE | ILE | LYS | THR | ALA | ||||
20 | GLY | ASN | GLY | GLN | PHE | LYS | ALA | VAL | GLY | ASP | ||||
21 | SER | LEU | GLU | ALA | GLN | GLN | TYR | GLY | ILE | ALA | ||||
22 | PHE | PRO | LYS | GLY | SER | ASP | GLU | GLN | ARG | ASP | ||||
23 | LYS | VAL | ASN | GLY | ALA | LEU | LYS | THR | LEU | ARG | ||||
24 | GLU | ASN | GLY | THR | TYR | ASN | GLU | ILE | TYR | LYS | ||||
25 | LYS | TRP | PHE | GLY | THR | GLU | PRO | LYS |
Samples:
sample_1: Glutamine binding protein (GlnBP), [U-100% 15N], 500 uM
sample_conditions_1: ionic strength: 0.003 M; pH: 7.5; pressure: 1 atm; temperature: 310 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
MARS - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHZ MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts