BMRB Entry 26821
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26821
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Title: apoTrpR PubMed: 28120439
Deposition date: 2016-06-20 Original release date: 2016-07-20
Authors: Gurla, Swapna; Montelione, Gaetano; Balasubramanian, Harish; Carey, Jannette; Kornhaber, Gregory; NESG, NE Struct. Genomics Consortium
Citation: Harish, Balasubramanian; Swapna, G.; Kornhaber, Gregory; Montelione, Gaetano; Carey, Jannette. "Multiple helical conformations of the helix-turn-helix region revealed by NOE-restrained MD simulations of tryptophan aporepressor, TrpR" Proteins 85, 731-740 (2017).
Assembly members:
apo_TrpR, polymer, 108 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
apo_TrpR: MAQQSPYSAAMAEQRHQEWL
RFVDLLKNAYQNDLHLPLLN
LMLTPDEREALGTRVRIVEE
LLRGEMSQRELKNELGAGIA
TITRGSNSLKAAPVELRQWL
EEVLLKSD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 218 |
| 15N chemical shifts | 90 |
| 1H chemical shifts | 417 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TrpR, sununit 1 | 1 |
Entities:
Entity 1, TrpR, sununit 1 108 residues - Formula weight is not available
| 1 | MET | ALA | GLN | GLN | SER | PRO | TYR | SER | ALA | ALA | ||||
| 2 | MET | ALA | GLU | GLN | ARG | HIS | GLN | GLU | TRP | LEU | ||||
| 3 | ARG | PHE | VAL | ASP | LEU | LEU | LYS | ASN | ALA | TYR | ||||
| 4 | GLN | ASN | ASP | LEU | HIS | LEU | PRO | LEU | LEU | ASN | ||||
| 5 | LEU | MET | LEU | THR | PRO | ASP | GLU | ARG | GLU | ALA | ||||
| 6 | LEU | GLY | THR | ARG | VAL | ARG | ILE | VAL | GLU | GLU | ||||
| 7 | LEU | LEU | ARG | GLY | GLU | MET | SER | GLN | ARG | GLU | ||||
| 8 | LEU | LYS | ASN | GLU | LEU | GLY | ALA | GLY | ILE | ALA | ||||
| 9 | THR | ILE | THR | ARG | GLY | SER | ASN | SER | LEU | LYS | ||||
| 10 | ALA | ALA | PRO | VAL | GLU | LEU | ARG | GLN | TRP | LEU | ||||
| 11 | GLU | GLU | VAL | LEU | LEU | LYS | SER | ASP |
Samples:
sample_1: apo TrpR, [U-100% 13C; U-100% 15N], 0.5 mM; Tris-HCl buffer 10 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 100 mM; pH: 5.7; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
AutoAssign v2.1.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
TOPSPIN v2.3, Bruker Biospin - collection
NMRPipe v2.1, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY v3.0, Goddard - data analysis, peak picking
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts