BMRB Entry 19881
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19881
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: transport protein m PubMed: 25090434
Deposition date: 2014-03-31 Original release date: 2015-04-13
Authors: Zhang, Yi; Hu, Yunfei; Jin, Changwen
Citation: Zhang, Yi; Hu, Yunfei; Li, Hongwei; Jin, Changwen. "Structural basis for TatA oligomerization: an NMR study of Escherichia coli TatA dimeric structure" Plos One 9, e103157-e103157 (2014).
Assembly members:
entity, polymer, 97 residues, 5024.057 Da.
Natural source: Common Name: E. Coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: MGGISIWQLLIIAVIVVLLF
GTKKLGSIGSDLGASIKGFK
KAMSDDEPKQDKTSQDADFT
AKTIADKQADTNQEQAKTED
AKRHDKEQVLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 370 |
| 15N chemical shifts | 90 |
| 1H chemical shifts | 628 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 97 residues - 5024.057 Da.
| 1 | MET | GLY | GLY | ILE | SER | ILE | TRP | GLN | LEU | LEU | ||||
| 2 | ILE | ILE | ALA | VAL | ILE | VAL | VAL | LEU | LEU | PHE | ||||
| 3 | GLY | THR | LYS | LYS | LEU | GLY | SER | ILE | GLY | SER | ||||
| 4 | ASP | LEU | GLY | ALA | SER | ILE | LYS | GLY | PHE | LYS | ||||
| 5 | LYS | ALA | MET | SER | ASP | ASP | GLU | PRO | LYS | GLN | ||||
| 6 | ASP | LYS | THR | SER | GLN | ASP | ALA | ASP | PHE | THR | ||||
| 7 | ALA | LYS | THR | ILE | ALA | ASP | LYS | GLN | ALA | ASP | ||||
| 8 | THR | ASN | GLN | GLU | GLN | ALA | LYS | THR | GLU | ASP | ||||
| 9 | ALA | LYS | ARG | HIS | ASP | LYS | GLU | GLN | VAL | LEU | ||||
| 10 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: entity, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 50 mM; DPC 200 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.05 M; pH: 7; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - data analysis
TOPSPIN, Bruker Biospin - collection
X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 700 MHz
- Bruker Avance 600 MHz
Related Database Links:
| BMRB | 19714 |
| PDB | |
| DBJ | BAB38189 BAE77465 BAG79648 BAI27909 BAI33032 |
| EMBL | CAA06724 CAP78301 CAQ34195 CAR00812 CAR05477 |
| GB | AAC19240 AAC76839 AAG59032 AAN45349 AAN83218 |
| PIR | D86071 |
| REF | NP_312793 NP_418280 NP_709642 WP_000508967 WP_001234791 |
| SP | P69428 P69429 P69430 P69431 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts