BMRB Entry 5060
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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/BMR5060
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: Yee, Adelinda; Chang, Xiaoqing; Pineda-Lucena, Antonio; Wu, Bin; Semesi, Anthony; Le, Brian; Ramelot, Theresa; Lee, Gregory; Bhattacharyya, Sudeepa; Gutierrez, Pablo; Denisov, Alexei; Lee, Chang-Hun; Cort, John; Kozlov, Guennadi; Liao, Jack; Finak, Grzegorz; Chen, Limin; Wishart, David; Lee, Weontae; McIntosh, Lawrence; Gehring, Kalle; Kennedy, Michael; Edwards, Aled; Arrowsmith, Cheryl. "An NMR approach to structural proteomics" Proc. Natl. Acad. Sci. U.S.A. 99, 1825-1830 (2002).
Assembly members:
TM006 protein from Thermotoga maritima, polymer, 98 residues, 11200 Da.
Natural source: Common Name: Thermotoga maritima Taxonomy ID: 2336 Superkingdom: Eubacteria Kingdom: not available Genus/species: Thermotoga maritima
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
TM006 protein from Thermotoga maritima: GSSHHHHHHSSGLVPRGSHM
AKYQVTKTLDVRGEVCPVPD
VETKRALQNMKPGEILEVWI
DYPMSKERIPETVKKLGHEV
LEIEEVGPSEWKIYIKVK
- assigned_chemical_shifts
- coupling_constants
| Data type | Count |
| 1H chemical shifts | 457 |
| 13C chemical shifts | 253 |
| 15N chemical shifts | 81 |
| coupling constants | 79 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TM006 | 1 |
Entities:
Entity 1, TM006 98 residues - 11200 Da.
| 1 | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | SER | ||||
| 2 | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | MET | ||||
| 3 | ALA | LYS | TYR | GLN | VAL | THR | LYS | THR | LEU | ASP | ||||
| 4 | VAL | ARG | GLY | GLU | VAL | CYS | PRO | VAL | PRO | ASP | ||||
| 5 | VAL | GLU | THR | LYS | ARG | ALA | LEU | GLN | ASN | MET | ||||
| 6 | LYS | PRO | GLY | GLU | ILE | LEU | GLU | VAL | TRP | ILE | ||||
| 7 | ASP | TYR | PRO | MET | SER | LYS | GLU | ARG | ILE | PRO | ||||
| 8 | GLU | THR | VAL | LYS | LYS | LEU | GLY | HIS | GLU | VAL | ||||
| 9 | LEU | GLU | ILE | GLU | GLU | VAL | GLY | PRO | SER | GLU | ||||
| 10 | TRP | LYS | ILE | TYR | ILE | LYS | VAL | LYS |
Samples:
sample_1: TM006 protein from Thermotoga maritima, [U-99% 13C; U-99% 15N], 2 mM; H20 90%; D20 10%
sample_2: TM006 protein from Thermotoga maritima, [U-99% 15N], 2 mM; H20 90%; D20 10%
sample_3: TM006 protein from Thermotoga maritima 5 mM; H20 90%; D20 10%
Ex-cond_1: pH: 6.8; temperature: 310 K; ionic strength: 0.15 M
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | not available | not available | not available |
| 3D CBCA(CO)HN | not available | not available | not available |
| 3D HNCO | not available | not available | not available |
| 3D HN(CA)CO | not available | not available | not available |
| 3D HNHA | not available | not available | not available |
| 3D 15N-HMQC-NOESY | not available | not available | not available |
| 3D 15N-HMQC-TOCSY | not available | not available | not available |
| 2D NOESY | not available | not available | not available |
| 2D TOCSY | not available | not available | not available |
| 2D 15N-HSQC | not available | not available | not available |
| 2D 13C-HSQC | not available | not available | not available |
Software:
XWINNMR v2.1 - data collection, data processing
XEASY v1.3.13 - data analysis
ARIA v14.5.98 - data analysis
NMR spectrometers:
- Bruker DRX 500 MHz
Related Database Links:
| PDB | |
| GB | AAD36062 ABQ47759 ACB10143 ACM23771 ADA67833 |
| REF | NP_228791 WP_004080581 WP_013932246 WP_015920041 YP_001245335 |
| SP | Q9X078 |
| AlphaFold | Q9X078 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks