BMRB Entry 15269
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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/BMR15269
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Title: Complete resonance assignments and solution structure calcualtion of ATC2521 (NESG ID: AtT6) from Agrobacterium tumeraciens
Deposition date: 2007-05-29 Original release date: 2007-07-05
Authors: Srisailam, Sampath; Lemak, Alexander; Yee, Adelinda; Karra, Murthy; Lukin, Jonathan; Arrowsmith, Cheryl
Citation: Srisailam, Sampath; Lemak, Alexander; Yee, Adelinda; Karra, Murthy; Lukin, Jonathan; Arrowsmith, Cheryl. "Solution Structure of a protein (ATC2521)of unknow function from Agrobacterium tumefaciens" Not known ., .-..
Assembly members:
ATC2521, polymer, 188 residues, 11548.9 Da.
Natural source: Common Name: Agrobacterium tumefaciens Taxonomy ID: 358 Superkingdom: Bacteria Kingdom: not available Genus/species: Agrobacterium tumefaciens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
ATC2521: MGSSHHHHHHSSGRENLYFQ
GHMNATIREILAKFGQLPTP
VDTIADEADLYAAGLSSFAS
VQLMLGIEEAFDIEFPDNLL
NRKSFASIKAIEDTVKLILD
GKEAAMNATIREILAKFGQL
PTPVDTIADEADLYAAGLSS
FASVQLMLGIEEAFDIEFPD
NLLNRKSFASIKAIEDTVKL
ILDGKEAA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 335 |
| 15N chemical shifts | 77 |
| 1H chemical shifts | 560 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ATC2521 | 1 |
Entities:
Entity 1, ATC2521 188 residues - 11548.9 Da.
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | ARG | GLU | ASN | LEU | TYR | PHE | GLN | ||||
| 3 | GLY | HIS | MET | ASN | ALA | THR | ILE | ARG | GLU | ILE | ||||
| 4 | LEU | ALA | LYS | PHE | GLY | GLN | LEU | PRO | THR | PRO | ||||
| 5 | VAL | ASP | THR | ILE | ALA | ASP | GLU | ALA | ASP | LEU | ||||
| 6 | TYR | ALA | ALA | GLY | LEU | SER | SER | PHE | ALA | SER | ||||
| 7 | VAL | GLN | LEU | MET | LEU | GLY | ILE | GLU | GLU | ALA | ||||
| 8 | PHE | ASP | ILE | GLU | PHE | PRO | ASP | ASN | LEU | LEU | ||||
| 9 | ASN | ARG | LYS | SER | PHE | ALA | SER | ILE | LYS | ALA | ||||
| 10 | ILE | GLU | ASP | THR | VAL | LYS | LEU | ILE | LEU | ASP | ||||
| 11 | GLY | LYS | GLU | ALA | ALA | MET | ASN | ALA | THR | ILE | ||||
| 12 | ARG | GLU | ILE | LEU | ALA | LYS | PHE | GLY | GLN | LEU | ||||
| 13 | PRO | THR | PRO | VAL | ASP | THR | ILE | ALA | ASP | GLU | ||||
| 14 | ALA | ASP | LEU | TYR | ALA | ALA | GLY | LEU | SER | SER | ||||
| 15 | PHE | ALA | SER | VAL | GLN | LEU | MET | LEU | GLY | ILE | ||||
| 16 | GLU | GLU | ALA | PHE | ASP | ILE | GLU | PHE | PRO | ASP | ||||
| 17 | ASN | LEU | LEU | ASN | ARG | LYS | SER | PHE | ALA | SER | ||||
| 18 | ILE | LYS | ALA | ILE | GLU | ASP | THR | VAL | LYS | LEU | ||||
| 19 | ILE | LEU | ASP | GLY | LYS | GLU | ALA | ALA |
Samples:
sample_1: ATC2521, [U-100% 13C; U-100% 15N], 1 ± 0.2 mM; TRIS 10 ± 0.2 mM; glycerol 5 ± 0.2 %; Benzamidine 1 ± 0.2 mM; sodium chloride 300 ± 0.2 mM; sodium azide 0.01 ± 0.1 %
sample_2: ATC2521, [U-100% 13C; U-100% 15N], 1 ± 0.2 mM; TRIS 10 ± 0.2 mM; glycerol 5 ± 0.2 %; Benzamidine 1 ± 0.2 mM; sodium chloride 300 ± 0.2 mM; sodium azide 0.01 ± 0.1 %
sample_conditions_1: ionic strength: 0.3 M; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(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 HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | 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 HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - data analysis, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts