BMRB Entry 16476
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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/BMR16476
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Title: Solution structure of protein Atu0922 from A. tumefaciens. Northeast Structural Genomics Consortium target AtT13. Ontario Center for Structural Proteomics target ATC0905.
Deposition date: 2009-09-02 Original release date: 2009-11-04
Authors: Gutmanas, Aleksandras; Yee, Adelinda; Lemak, Alexander; Fares, Christophe; Semesi, Anthony; Arrowsmith, Cheryl
Citation: Gutmanas, Aleksandras; Lemak, Alexander; Yee, Adelinda; Semesi, Anthony; Fares, Christophe; Arrowsmith, Cheryl. "Solution NMR structure of protein atc0905 from A. tumefaciens." To be published ., .-..
Assembly members:
ATC0905, polymer, 121 residues, Formula weight is not available
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):
ATC0905: QGHMRLKSEMFVSALIRRVF
AAGGFAAVEKKGAEAAGAIF
VRQRLRDGRENLYGPAPQSF
ADDEDIMRAERRFETRLAGV
EGEEIAALLERERRFDSDLW
VVEIETDEIGTLLTLVDQPQ
A
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 514 |
| 15N chemical shifts | 122 |
| 1H chemical shifts | 829 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ATC0905 | 1 |
Entities:
Entity 1, ATC0905 121 residues - Formula weight is not available
| 1 | GLN | GLY | HIS | MET | ARG | LEU | LYS | SER | GLU | MET | ||||
| 2 | PHE | VAL | SER | ALA | LEU | ILE | ARG | ARG | VAL | PHE | ||||
| 3 | ALA | ALA | GLY | GLY | PHE | ALA | ALA | VAL | GLU | LYS | ||||
| 4 | LYS | GLY | ALA | GLU | ALA | ALA | GLY | ALA | ILE | PHE | ||||
| 5 | VAL | ARG | GLN | ARG | LEU | ARG | ASP | GLY | ARG | GLU | ||||
| 6 | ASN | LEU | TYR | GLY | PRO | ALA | PRO | GLN | SER | PHE | ||||
| 7 | ALA | ASP | ASP | GLU | ASP | ILE | MET | ARG | ALA | GLU | ||||
| 8 | ARG | ARG | PHE | GLU | THR | ARG | LEU | ALA | GLY | VAL | ||||
| 9 | GLU | GLY | GLU | GLU | ILE | ALA | ALA | LEU | LEU | GLU | ||||
| 10 | ARG | GLU | ARG | ARG | PHE | ASP | SER | ASP | LEU | TRP | ||||
| 11 | VAL | VAL | GLU | ILE | GLU | THR | ASP | GLU | ILE | GLY | ||||
| 12 | THR | LEU | LEU | THR | LEU | VAL | ASP | GLN | PRO | GLN | ||||
| 13 | ALA |
Samples:
sample: ATC0905, [U-100% 13C; U-100% 15N], 1 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; DTT 10 mM; benzamidine 1 uM; Roche inhibitor coctail 1 x; D2O 10%; H2O 90%
sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample | isotropic | sample_conditions_1 |
| 3D HNCO | sample | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample | isotropic | sample_conditions_1 |
| 3D HNCA | sample | isotropic | sample_conditions_1 |
| 3D 1H-13C arom NOESY | sample | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample | isotropic | sample_conditions_1 |
| 3D 1H-13C aliph NOESY | sample | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample | isotropic | sample_conditions_1 |
| 3D H(C)CH-TOCSY aliphatic | sample | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY aliphatic | sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC CT | sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC arom | sample | isotropic | sample_conditions_1 |
| 2D HBCBCGCDHD | sample | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
VNMRJ, Varian - collection
ABACUS, Lemak, A - chemical shift assignment
MDDNMR, Orekhov, V. Yu. - processing
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
Analysis, CCPN - data analysis, peak picking
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| GB | AAK86727 EGL65971 KEY55322 KJX89147 |
| REF | NP_353942 WP_006311220 WP_010971254 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts