BMRB Entry 16979
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16979
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Title: Solution structure of Enzyme IIB subunit of PTS system from Escherichia coli K12. Northeast Structural Genomics Consortium target ER315/Ontario Center for Structural Proteomics target ec0544
Deposition date: 2010-06-07 Original release date: 2010-06-24
Authors: Wu, Bin; Yee, Adelinda; Gutmanas, Aleksandras; Semest, Anthony; Arrowsmith, Cheryl
Citation: Wu, Bin; Yee, Adelinda; Gutmanas, Aleksandras; Semest, Anthony; Arrowsmith, Cheryl. "Solution structure of Enzyme IIB subunit of PTS system from Escherichia coli K12. Northeast Structural Genomics Consortium target ER315/Ontario Center for Structural Proteomics target ec0544" Not known ., .-..
Assembly members:
ec0544, polymer, 108 residues, 11745.361 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
ec0544: MSKKLIALCACPMGLAHTFM
AAQALEEAAVEAGYEVKIET
QGADGIQNRLTAQDIAEATI
IIHSVAVTPEDNERFESRDV
YEITLQDAIKNAAGIIKEIE
EMIASEQQ
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 452 |
| 15N chemical shifts | 115 |
| 1H chemical shifts | 762 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ec0544 | 1 |
Entities:
Entity 1, ec0544 108 residues - 11745.361 Da.
| 1 | MET | SER | LYS | LYS | LEU | ILE | ALA | LEU | CYS | ALA | ||||
| 2 | CYS | PRO | MET | GLY | LEU | ALA | HIS | THR | PHE | MET | ||||
| 3 | ALA | ALA | GLN | ALA | LEU | GLU | GLU | ALA | ALA | VAL | ||||
| 4 | GLU | ALA | GLY | TYR | GLU | VAL | LYS | ILE | GLU | THR | ||||
| 5 | GLN | GLY | ALA | ASP | GLY | ILE | GLN | ASN | ARG | LEU | ||||
| 6 | THR | ALA | GLN | ASP | ILE | ALA | GLU | ALA | THR | ILE | ||||
| 7 | ILE | ILE | HIS | SER | VAL | ALA | VAL | THR | PRO | GLU | ||||
| 8 | ASP | ASN | GLU | ARG | PHE | GLU | SER | ARG | ASP | VAL | ||||
| 9 | TYR | GLU | ILE | THR | LEU | GLN | ASP | ALA | ILE | LYS | ||||
| 10 | ASN | ALA | ALA | GLY | ILE | ILE | LYS | GLU | ILE | GLU | ||||
| 11 | GLU | MET | ILE | ALA | SER | GLU | GLN | GLN |
Samples:
sample_1: ec0544, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; zinc sulphate 10 uM; DTT, [U-100% 2H], 10 mM; benzamidine 10 mM; inhibitor cocktail 1; H2O 90%; D2O 10%
sample_2: ec0544, [U-7% 13C; U-100% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; zinc sulphate 10 uM; DTT, [U-100% 2H], 10 mM; benzamidine 10 mM; inhibitor cocktail 1 x; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 300 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
MDDGUI v1.0, Gutmanas, Arrowsmith - processing
SPARKY v3.95, Goddard - data analysis, peak picking
FAWN v1.0, Lemak, Arrowsmith - chemical shift assignment
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
AutoStruct, Huang, Tejero, Powers and Montelione - NMR structure quality assessment
PSVS, Bhattacharya and Montelione - NMR structure quality assessment
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAA16257 BAB36690 BAG78208 BAI26647 BAI31678 |
| EMBL | CAP76866 CAQ32775 CAQ88317 CAQ99295 CAR03856 |
| GB | AAC75446 AAG57513 AAN43961 AAN81376 AAP17772 |
| REF | NP_311294 NP_416888 NP_708254 WP_000038452 WP_000038453 |
| SP | P69808 P69809 P69810 Q821A9 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts