BMRB Entry 15735
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15735
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Slynko, Vadim; Schubert, Mario; Numao, Shin; Kowarik, Michael; Aebi, Markus; Allain, Frederic. "NMR structure determination of a segmentally labeled glycoprotein using in vitro glycosylation" J. Am. Chem. Soc. 131, 1274-1281 (2009).
PubMed: 19154179
Assembly members:
AcrA(61-210DD), polymer, 116 residues, 12748.376 Da.
Natural source: Common Name: Campylobacter jejuni Taxonomy ID: 197 Superkingdom: Bacteria Kingdom: not available Genus/species: Campylobacter jejuni
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET24b
Entity Sequences (FASTA):
AcrA(61-210DD): DVIIKPQVSGVIVNKLFKAG
DKVKKGQTLFIIEQDQASKD
FNRSKALFSQSAISQKEYDS
SLATLDHTEIKAPFDGTIGD
ALVNIGDYVSASTTELVRVT
NLNPIYADGSHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 332 |
| 15N chemical shifts | 117 |
| 1H chemical shifts | 752 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 116 residues - 12748.376 Da.
The construct consists of residues 61-210 of AcrA of C. jejuni with deletions of res. 97-117 and 146-166 and two mutations: K96Q K131Q.
| 1 | ASP | VAL | ILE | ILE | LYS | PRO | GLN | VAL | SER | GLY | ||||
| 2 | VAL | ILE | VAL | ASN | LYS | LEU | PHE | LYS | ALA | GLY | ||||
| 3 | ASP | LYS | VAL | LYS | LYS | GLY | GLN | THR | LEU | PHE | ||||
| 4 | ILE | ILE | GLU | GLN | ASP | GLN | ALA | SER | LYS | ASP | ||||
| 5 | PHE | ASN | ARG | SER | LYS | ALA | LEU | PHE | SER | GLN | ||||
| 6 | SER | ALA | ILE | SER | GLN | LYS | GLU | TYR | ASP | SER | ||||
| 7 | SER | LEU | ALA | THR | LEU | ASP | HIS | THR | GLU | ILE | ||||
| 8 | LYS | ALA | PRO | PHE | ASP | GLY | THR | ILE | GLY | ASP | ||||
| 9 | ALA | LEU | VAL | ASN | ILE | GLY | ASP | TYR | VAL | SER | ||||
| 10 | ALA | SER | THR | THR | GLU | LEU | VAL | ARG | VAL | THR | ||||
| 11 | ASN | LEU | ASN | PRO | ILE | TYR | ALA | ASP | GLY | SER | ||||
| 12 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: AcrA(61-210DD), [U-100% 15N], 1 mM; potassium phosphate 50 mM
sample_2: AcrA(61-210DD), [U-100% 13C; U-100% 15N], 1 mM; potassium phosphate 50 mM
sample_3: AcrA(61-210DD), [U-100% 15N], 1 mM; potassium phosphate 50 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6.4; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
AMBER v8, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement
ATHNOS-CANDID, Herrmann, Guntert, Wuthrich - geometry optimization
SPARKY, Goddard - chemical shift assignment
TOPSPIN v2.0, Bruker Biospin - processing
NMR spectrometers:
- Bruker Avance 900 MHz
- Bruker Avance 750 MHz
- Bruker Avance 600 MHz
- Bruker Avance 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks