BMRB Entry 15028
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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/BMR15028
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Title: 1H, 13C, and 15N Chemical Shift Assignments of Trx-ArsC complex PubMed: 17303556
Deposition date: 2006-11-13 Original release date: 2008-06-23
Authors: Jin, Changwen; Hu, Yunfei; Li, You; Zhang, Xinxin
Citation: Li, Y.; Hu, Y.; Zhang, X.; Xu, H.; Lescop, E.; Xia, B.; Jin, C.. "Conformational fluctuations coupled to the thiol-disulfide transfer between thioredoxin and arsenate reductase in Bacillus subtilis" J. Biol. Chem. 282, 11078-11083 (2007).
Assembly members:
thioredoxin, polymer, 104 residues, 11377.1 Da.
arsenate_reductase, polymer, 139 residues, 15531.3 Da.
Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
thioredoxin: MAIVKATDQSFSAETSEGVV
LADFWAPWCGPSKMIAPVLE
ELDQEMGDKLKIVKIDVDEN
QETAGKYGVMSIPTLLVLKD
GEVVETSVGFKPKEALQELV
NKHL
arsenate_reductase: MENKIIYFLSTGNSARSQMA
EGWAKQYLGDEWKVYSAGIE
AHGLNPNAVKAMKEVGIDIS
NQTSDIIDSDILNNADLVVT
LSGDAADKCPMTPPHVKREH
WGFDDPARAQGTEEEKWAFF
QRVRDEIGNRLKEFAETGK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 740 |
| 15N chemical shifts | 249 |
| 1H chemical shifts | 1543 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | thioredoxin | 1 |
| 2 | arsenate_reductase | 2 |
Entities:
Entity 1, thioredoxin 104 residues - 11377.1 Da.
| 1 | MET | ALA | ILE | VAL | LYS | ALA | THR | ASP | GLN | SER | ||||
| 2 | PHE | SER | ALA | GLU | THR | SER | GLU | GLY | VAL | VAL | ||||
| 3 | LEU | ALA | ASP | PHE | TRP | ALA | PRO | TRP | CYS | GLY | ||||
| 4 | PRO | SER | LYS | MET | ILE | ALA | PRO | VAL | LEU | GLU | ||||
| 5 | GLU | LEU | ASP | GLN | GLU | MET | GLY | ASP | LYS | LEU | ||||
| 6 | LYS | ILE | VAL | LYS | ILE | ASP | VAL | ASP | GLU | ASN | ||||
| 7 | GLN | GLU | THR | ALA | GLY | LYS | TYR | GLY | VAL | MET | ||||
| 8 | SER | ILE | PRO | THR | LEU | LEU | VAL | LEU | LYS | ASP | ||||
| 9 | GLY | GLU | VAL | VAL | GLU | THR | SER | VAL | GLY | PHE | ||||
| 10 | LYS | PRO | LYS | GLU | ALA | LEU | GLN | GLU | LEU | VAL | ||||
| 11 | ASN | LYS | HIS | LEU |
Entity 2, arsenate_reductase 139 residues - 15531.3 Da.
| 1 | MET | GLU | ASN | LYS | ILE | ILE | TYR | PHE | LEU | SER | ||||
| 2 | THR | GLY | ASN | SER | ALA | ARG | SER | GLN | MET | ALA | ||||
| 3 | GLU | GLY | TRP | ALA | LYS | GLN | TYR | LEU | GLY | ASP | ||||
| 4 | GLU | TRP | LYS | VAL | TYR | SER | ALA | GLY | ILE | GLU | ||||
| 5 | ALA | HIS | GLY | LEU | ASN | PRO | ASN | ALA | VAL | LYS | ||||
| 6 | ALA | MET | LYS | GLU | VAL | GLY | ILE | ASP | ILE | SER | ||||
| 7 | ASN | GLN | THR | SER | ASP | ILE | ILE | ASP | SER | ASP | ||||
| 8 | ILE | LEU | ASN | ASN | ALA | ASP | LEU | VAL | VAL | THR | ||||
| 9 | LEU | SER | GLY | ASP | ALA | ALA | ASP | LYS | CYS | PRO | ||||
| 10 | MET | THR | PRO | PRO | HIS | VAL | LYS | ARG | GLU | HIS | ||||
| 11 | TRP | GLY | PHE | ASP | ASP | PRO | ALA | ARG | ALA | GLN | ||||
| 12 | GLY | THR | GLU | GLU | GLU | LYS | TRP | ALA | PHE | PHE | ||||
| 13 | GLN | ARG | VAL | ARG | ASP | GLU | ILE | GLY | ASN | ARG | ||||
| 14 | LEU | LYS | GLU | PHE | ALA | GLU | THR | GLY | LYS |
Samples:
sample_1: Trx-ArsC complex, [U-13C; U-15N], 1 – 2 mM; Trx-ArsC complex1 – 2 mM; Tris-HCl 20 mM; Na2SO4 20 mM; KCL 40 mM
sample_2: Trx-ArsC complex mM; Trx-ArsC complex, [U-13C; U-15N], mM; Tris-HCl 20 mM; Na2SO4 20 mM; KCL 40 mM
sample_conditions_1: ionic strength: 0.08 M; pH: 6.85; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRView, B Johnson, One Moon Scientific - chemical shift assignment
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAI86356 BAM54098 BAM58927 GAK79977 BAA06970 BAA12434 BAM58640 |
| EMBL | CAA99577 CAB14810 CBI43781 CCF06106 CCG50792 CAB14519 CEI57801 CEJ78223 |
| GB | AAA87315 ABS74914 ADM38802 ADP33333 ADV93643 ADV93326 AFH58698 AFH58699 AFH58701 AFH58702 |
| REF | NP_390728 WP_003152560 WP_003222500 WP_003325184 WP_014664890 NP_390455 WP_004398596 WP_029318100 YP_004204353 YP_007534562 |
| SP | P14949 P45947 |
| BMRB | 6075 6563 |
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