BMRB Entry 30082
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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/BMR30082
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Title: The structure of chaperone SecB in complex with unstructured proPhoA binding site c PubMed: 27501151
Deposition date: 2016-05-09 Original release date: 2016-08-18
Authors: Huang, C.; Saio, T.; Rossi, P.; Kalodimos, C.
Citation: Huang, C.; Saio, T.; Rossi, P.; Kalodimos, C.. "Structural basis for the antifolding activity of a molecular chaperone" Nature 537, 202-206 (2016).
Assembly members:
Protein-export protein SecB, polymer, 155 residues, 17287.266 Da.
Alkaline phosphatase, polymer, 55 residues, 5732.327 Da.
Natural source: Common Name: enterobacteria Taxonomy ID: 83334 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
Protein-export protein SecB: MSEQNNTEMTFQIQRIYTKD
ISFEAPNAPHVFQKDWQPEV
KLDLDTASSQLADDVYEVVL
RVTVTASLGEETAFLCEVQQ
GGIFSIAGIEGTQMAHCLGA
YCPNILFPYARECITSMVSR
GTFPQLNLAPVNFDALFMNY
LQQQAGEGTEEHQDA
Alkaline phosphatase: GGFFKGIDALPLTGQYTHYA
LNKKTGKPDYVTDSAASATA
WSTGVKTYNGALGVD
| Data type | Count |
| 13C chemical shifts | 2276 |
| 15N chemical shifts | 640 |
| 1H chemical shifts | 2024 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1, chain 1 | 1 |
| 2 | entity_1, chain 2 | 1 |
| 3 | entity_1, chain 3 | 1 |
| 4 | entity_1, chain 4 | 1 |
| 5 | entity_2, chain 1 | 2 |
| 6 | entity_2, chain 2 | 2 |
Entities:
Entity 1, entity_1, chain 1 155 residues - 17287.266 Da.
| 1 | MET | SER | GLU | GLN | ASN | ASN | THR | GLU | MET | THR | ||||
| 2 | PHE | GLN | ILE | GLN | ARG | ILE | TYR | THR | LYS | ASP | ||||
| 3 | ILE | SER | PHE | GLU | ALA | PRO | ASN | ALA | PRO | HIS | ||||
| 4 | VAL | PHE | GLN | LYS | ASP | TRP | GLN | PRO | GLU | VAL | ||||
| 5 | LYS | LEU | ASP | LEU | ASP | THR | ALA | SER | SER | GLN | ||||
| 6 | LEU | ALA | ASP | ASP | VAL | TYR | GLU | VAL | VAL | LEU | ||||
| 7 | ARG | VAL | THR | VAL | THR | ALA | SER | LEU | GLY | GLU | ||||
| 8 | GLU | THR | ALA | PHE | LEU | CYS | GLU | VAL | GLN | GLN | ||||
| 9 | GLY | GLY | ILE | PHE | SER | ILE | ALA | GLY | ILE | GLU | ||||
| 10 | GLY | THR | GLN | MET | ALA | HIS | CYS | LEU | GLY | ALA | ||||
| 11 | TYR | CYS | PRO | ASN | ILE | LEU | PHE | PRO | TYR | ALA | ||||
| 12 | ARG | GLU | CYS | ILE | THR | SER | MET | VAL | SER | ARG | ||||
| 13 | GLY | THR | PHE | PRO | GLN | LEU | ASN | LEU | ALA | PRO | ||||
| 14 | VAL | ASN | PHE | ASP | ALA | LEU | PHE | MET | ASN | TYR | ||||
| 15 | LEU | GLN | GLN | GLN | ALA | GLY | GLU | GLY | THR | GLU | ||||
| 16 | GLU | HIS | GLN | ASP | ALA |
Entity 2, entity_2, chain 1 55 residues - 5732.327 Da.
| 1 | GLY | GLY | PHE | PHE | LYS | GLY | ILE | ASP | ALA | LEU | ||||
| 2 | PRO | LEU | THR | GLY | GLN | TYR | THR | HIS | TYR | ALA | ||||
| 3 | LEU | ASN | LYS | LYS | THR | GLY | LYS | PRO | ASP | TYR | ||||
| 4 | VAL | THR | ASP | SER | ALA | ALA | SER | ALA | THR | ALA | ||||
| 5 | TRP | SER | THR | GLY | VAL | LYS | THR | TYR | ASN | GLY | ||||
| 6 | ALA | LEU | GLY | VAL | ASP |
Samples:
sample_1: E.coli Alkaline Phosphatase (PhoA) binding site c, [U-100% 13C; U-100% 15N], 300 uM; E.coli Chaperone SecB, [U-100% 13C; U-100% 15N], 300 uM; potassium chloride 150 mM; potassium phosphate 50 mM; sodium phosphate 50 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 150 mM; pH: 7; pressure: 1 atm; temperature: 301 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | 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 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment
NMR spectrometers:
- Bruker AvanceIII 700 MHz
- Varian INOVA 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts