BMRB Entry 5403
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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/BMR5403
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Title: Backbone resonance assignments of the 91 kDa oligomeric TRAP protein from Bacillus staerothermophilus in complex with L-tryptophan PubMed: 12381302
Deposition date: 2002-06-26 Original release date: 2003-04-10
Authors: McElroy, Craig; Manfredo, Amanda; Wendt, Alice; Gollnick, Paul; Foster, Mark
Citation: McElroy, Craig; Manfredo, Amanda; Wendt, Alice; Gollnick, Paul; Foster, Mark. "TROSY-NMR Studies of the 91 kDa TRAP Protein reveal Allosteric Control of a Gene Regulatory Protein by Ligand-altered Flexibility" J. Mol. Biol. 323, 463-473 (2002).
Assembly members:
trp RNA-binding attenuation protein, polymer, 74 residues, 8243 Da.
TRYPTOPHAN, non-polymer, 204.225 Da.
Natural source: Common Name: Geobacillus stearothermophilus Taxonomy ID: 1422 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus stearothermophilus
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
trp RNA-binding attenuation protein: MYTNSDFVVIKALEDGVNVI
GLTRGADTRFHHSEKLDKGE
VLIAQFTEHTSAIKVRGKAY
IQTRHGVIESEGKK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 148 |
| 15N chemical shifts | 57 |
| 1H chemical shifts | 57 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TRAP subunit A | 1 |
| 2 | TRAP subunit B | 1 |
| 3 | TRAP subunit C | 1 |
| 4 | TRAP subunit D | 1 |
| 5 | TRAP subunit E | 1 |
| 6 | TRAP subunit F | 1 |
| 7 | TRAP subunit G | 1 |
| 8 | TRAP subunit H | 1 |
| 9 | TRAP subunit I | 1 |
| 10 | TRAP subunit J | 1 |
| 11 | TRAP subunit K | 1 |
| 12 | L-tryptophan, 1 | 2 |
| 13 | L-tryptophan, 2 | 2 |
| 14 | L-tryptophan, 3 | 2 |
| 15 | L-tryptophan, 4 | 2 |
| 16 | L-tryptophan, 5 | 2 |
| 17 | L-tryptophan, 6 | 2 |
| 18 | L-tryptophan, 7 | 2 |
| 19 | L-tryptophan, 8 | 2 |
| 20 | L-tryptophan, 9 | 2 |
| 21 | L-tryptophan, 10 | 2 |
| 22 | L-tryptophan, 11 | 2 |
Entities:
Entity 1, TRAP subunit A 74 residues - 8243 Da.
| 1 | MET | TYR | THR | ASN | SER | ASP | PHE | VAL | VAL | ILE | ||||
| 2 | LYS | ALA | LEU | GLU | ASP | GLY | VAL | ASN | VAL | ILE | ||||
| 3 | GLY | LEU | THR | ARG | GLY | ALA | ASP | THR | ARG | PHE | ||||
| 4 | HIS | HIS | SER | GLU | LYS | LEU | ASP | LYS | GLY | GLU | ||||
| 5 | VAL | LEU | ILE | ALA | GLN | PHE | THR | GLU | HIS | THR | ||||
| 6 | SER | ALA | ILE | LYS | VAL | ARG | GLY | LYS | ALA | TYR | ||||
| 7 | ILE | GLN | THR | ARG | HIS | GLY | VAL | ILE | GLU | SER | ||||
| 8 | GLU | GLY | LYS | LYS |
Entity 2, L-tryptophan, 1 - C11 H12 N2 O2 - 204.225 Da.
| 1 | TRP |
Samples:
sample_1: trp RNA-binding attenuation protein, [U-2H; U-13C; U-15N], 6.6 mM; L-TRYPTOPHAN, [U-2H; U-13C; U-15N], 6.6 mM
condition_1: pH: 8.0; temperature: 328 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| TROSY | sample_1 | not available | condition_1 |
| TROSY-HNCA | sample_1 | not available | condition_1 |
| TROSY-HN(CO)CA | sample_1 | not available | condition_1 |
| TROSY-HNCACB | sample_1 | not available | condition_1 |
| TROSY-HNCO | sample_1 | not available | condition_1 |
Software:
No software information available
NMR spectrometers:
- Bruker DRX 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAD76498 |
| GenBank | AAD33793 ABO67499 |
| REF | YP_001126244 YP_148066 |
| SWISS-PROT | Q9X6J6 |
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