BMRB Entry 6369
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6369
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Title: 1H, 13C 15N chemical shift assignment Bacillus halodurans Protein BH1534: The Northeast Structural Genomics Consortium Target BhR29 PubMed: 16027363
Deposition date: 2004-10-27 Original release date: 2008-08-28
Authors: Liu, Gaohua; Ma, Lichung; Shen, Yang; Acton, Thomas; Atreya, Hanudatta; Xiao, Rong; Montelione, Gaetano; Szyperski, Thomas
Citation: Liu, Gaohua; Shen, Yang; Atreya, Hanudatta; Parish, David; Shao, Ying; Sukumaran, Dinesh; Xiao, Rong; Yee, Adelinda; Lemak, Alexander; Bhattacharya, Aneerban; Acton, Thomas; Arrowsmith, Cheryl; Montelione, Gaetano; Szyperski, Thomas. "NMR data collection and analysis protocol for high-throughput protein structure determination" Proc. Natl. Acad. Sci. U.S.A. 102, 10487-10492 (2005).
Assembly members:
Protein BH1534, polymer, 138 residues, Formula weight is not available
Natural source: Common Name: Bacillus halodurans Taxonomy ID: 86665 Superkingdom: Bacteria Kingdom: Not applicable Genus/species: Bacillus halodurans
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
Protein BH1534: MTRLPDIKKEVRFNAPIEKV
WEAVSTSEGLAFWFMENDLK
AETGHHFHLQSPFGPSPCQV
TDVERPIKLSFTWDTDGWSV
TFHLKEEENGTIFTIVHSGW
KQGDTKVEKAGAESAVVHER
MDRGWHDLVNERLRQIVE
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 988 |
| 13C chemical shifts | 501 |
| 15N chemical shifts | 148 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Protein BH1534 | 1 |
Entities:
Entity 1, Protein BH1534 138 residues - Formula weight is not available
| 1 | MET | THR | ARG | LEU | PRO | ASP | ILE | LYS | LYS | GLU | ||||
| 2 | VAL | ARG | PHE | ASN | ALA | PRO | ILE | GLU | LYS | VAL | ||||
| 3 | TRP | GLU | ALA | VAL | SER | THR | SER | GLU | GLY | LEU | ||||
| 4 | ALA | PHE | TRP | PHE | MET | GLU | ASN | ASP | LEU | LYS | ||||
| 5 | ALA | GLU | THR | GLY | HIS | HIS | PHE | HIS | LEU | GLN | ||||
| 6 | SER | PRO | PHE | GLY | PRO | SER | PRO | CYS | GLN | VAL | ||||
| 7 | THR | ASP | VAL | GLU | ARG | PRO | ILE | LYS | LEU | SER | ||||
| 8 | PHE | THR | TRP | ASP | THR | ASP | GLY | TRP | SER | VAL | ||||
| 9 | THR | PHE | HIS | LEU | LYS | GLU | GLU | GLU | ASN | GLY | ||||
| 10 | THR | ILE | PHE | THR | ILE | VAL | HIS | SER | GLY | TRP | ||||
| 11 | LYS | GLN | GLY | ASP | THR | LYS | VAL | GLU | LYS | ALA | ||||
| 12 | GLY | ALA | GLU | SER | ALA | VAL | VAL | HIS | GLU | ARG | ||||
| 13 | MET | ASP | ARG | GLY | TRP | HIS | ASP | LEU | VAL | ASN | ||||
| 14 | GLU | ARG | LEU | ARG | GLN | ILE | VAL | GLU |
Samples:
sample_1: Protein BH1534, [U-13C; U-15N], 0.8 mM; MES 20 mM; NaCl 100 mM; DTT 10 mM; CaCl2 5 mM; NaN3 0.02%; H2O 95%; D2O 5%
sample_conditions: temperature: 298 K; pH: 6.5; pressure: 1 atm
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| GFT (4,3)D HNNCabCa | not available | not available | not available |
| GFT (4,3)D CabCacONHN | not available | not available | not available |
| GFT (4,3)D HabCabcoNHN | not available | not available | not available |
| GFT (4,3)HCCH and simutanously NOESY | not available | not available | not available |
Software:
No software information available
NMR spectrometers:
- Varian Inova 600 MHz
- Varian Inova 750 MHz
Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone
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