BMRB Entry 27037
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27037
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Title: Alanine chemical shifts of the N-terminal domain (residues 1-215) of HtpG, the Hsp90 from Escherichia coli. Northeast Structural Genomics Consortium Target ER697A. PubMed: 28653216
Deposition date: 2017-02-24 Original release date: 2017-06-30
Authors: Ramelot, Theresa; Pederson, Kari; Wang, Huang; Maglaqui, Melissa; Mao, Lei; Xiao, Rong; Acton, Thomas; Everett, John; Prestegard, James; Montelione, Gaetano; Kennedy, Michael
Citation: Pederson, Kari; Chalmers, Gordon; Gao, Qi; Elnatan, Daniel; Ramelot, Theresa; Ma, Li-Chung; Montelione, Gaetano; Kennedy, Michael; Agard, David; Prestegard, James. "NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with (13)C-methyl alanine" J. Biomol. NMR 68, 225-236 (2017).
Assembly members:
NTD, polymer, 214 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: pET15_NESG
Entity Sequences (FASTA):
NTD: KGQETRGFQSEVKQLLHLMI
HSLYSNKEIFLRELISNASD
AADKLRFRALSNPDLYEGDG
ELRVRVSFDKDKRTLTISDN
GVGMTRDEVIDHLGTIAKSG
TKSFLESLGSDQAKDSQLIG
QFGVGFYSAFIVADKVTVRT
RAAGEKPENGVFWESAGEGE
YTVADITKEDRGTEITLHLR
EGEDEFLDDWRVRSIISKYS
DHIALPVEIEKREE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 39 |
| 15N chemical shifts | 13 |
| 1H chemical shifts | 65 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NTD | 1 |
Entities:
Entity 1, NTD 214 residues - Formula weight is not available
10 N-terminal residues not included: MGHHHHHHSH
| 1 | LYS | GLY | GLN | GLU | THR | ARG | GLY | PHE | GLN | SER | ||||
| 2 | GLU | VAL | LYS | GLN | LEU | LEU | HIS | LEU | MET | ILE | ||||
| 3 | HIS | SER | LEU | TYR | SER | ASN | LYS | GLU | ILE | PHE | ||||
| 4 | LEU | ARG | GLU | LEU | ILE | SER | ASN | ALA | SER | ASP | ||||
| 5 | ALA | ALA | ASP | LYS | LEU | ARG | PHE | ARG | ALA | LEU | ||||
| 6 | SER | ASN | PRO | ASP | LEU | TYR | GLU | GLY | ASP | GLY | ||||
| 7 | GLU | LEU | ARG | VAL | ARG | VAL | SER | PHE | ASP | LYS | ||||
| 8 | ASP | LYS | ARG | THR | LEU | THR | ILE | SER | ASP | ASN | ||||
| 9 | GLY | VAL | GLY | MET | THR | ARG | ASP | GLU | VAL | ILE | ||||
| 10 | ASP | HIS | LEU | GLY | THR | ILE | ALA | LYS | SER | GLY | ||||
| 11 | THR | LYS | SER | PHE | LEU | GLU | SER | LEU | GLY | SER | ||||
| 12 | ASP | GLN | ALA | LYS | ASP | SER | GLN | LEU | ILE | GLY | ||||
| 13 | GLN | PHE | GLY | VAL | GLY | PHE | TYR | SER | ALA | PHE | ||||
| 14 | ILE | VAL | ALA | ASP | LYS | VAL | THR | VAL | ARG | THR | ||||
| 15 | ARG | ALA | ALA | GLY | GLU | LYS | PRO | GLU | ASN | GLY | ||||
| 16 | VAL | PHE | TRP | GLU | SER | ALA | GLY | GLU | GLY | GLU | ||||
| 17 | TYR | THR | VAL | ALA | ASP | ILE | THR | LYS | GLU | ASP | ||||
| 18 | ARG | GLY | THR | GLU | ILE | THR | LEU | HIS | LEU | ARG | ||||
| 19 | GLU | GLY | GLU | ASP | GLU | PHE | LEU | ASP | ASP | TRP | ||||
| 20 | ARG | VAL | ARG | SER | ILE | ILE | SER | LYS | TYR | SER | ||||
| 21 | ASP | HIS | ILE | ALA | LEU | PRO | VAL | GLU | ILE | GLU | ||||
| 22 | LYS | ARG | GLU | GLU |
Samples:
sample_1: NTD, [U-100% 13C; U-100% 15N], 0.49 mM; TRIS 10 mM; sodium chloride 100 mM; sodium azide 0.02%; DTT 10 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC NH2 only | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC CT aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
SPARKY, Goddard - peak picking
VNMR, Varian - collection
TOPSPIN v2.1, Bruker Biospin - collection
NMR spectrometers:
- Varian INOVA 600 MHz
- Bruker Avance 850 MHz
- Bruker Avance 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts