Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19713
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: Ghasriani, Houman; Kwok, Jason; Sherrat, Allison; Foo, Alexander; Qureshi, Tabussom; Goto, Natalie. "Micelle-Catalyzed Domain Swapping in the GlpG Rhomboid Protease Cytoplasmic Domain" Biochemistry 53, 5907-5915 (2014).
PubMed: 25162988
Assembly members:
Domain_Swapped_GLPG, polymer, 63 residues, 7156.092 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 Vector: PET 30A +
Entity Sequences (FASTA):
Domain_Swapped_GLPG: MLMITSFANPRVAQAFVDYM
ATQGVILTIQQHNQSDVWLA
DESQAERVRAELARFLENPA
DLE
| Data type | Count |
| 13C chemical shifts | 193 |
| 15N chemical shifts | 69 |
| 1H chemical shifts | 429 |
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Domain_Swapped_GLPG_1 | 1 |
| 2 | Domain_Swapped_GLPG_2 | 1 |
Entity 1, Domain_Swapped_GLPG_1 63 residues - 7156.092 Da.
| 1 | MET | LEU | MET | ILE | THR | SER | PHE | ALA | ASN | PRO | ||||
| 2 | ARG | VAL | ALA | GLN | ALA | PHE | VAL | ASP | TYR | MET | ||||
| 3 | ALA | THR | GLN | GLY | VAL | ILE | LEU | THR | ILE | GLN | ||||
| 4 | GLN | HIS | ASN | GLN | SER | ASP | VAL | TRP | LEU | ALA | ||||
| 5 | ASP | GLU | SER | GLN | ALA | GLU | ARG | VAL | ARG | ALA | ||||
| 6 | GLU | LEU | ALA | ARG | PHE | LEU | GLU | ASN | PRO | ALA | ||||
| 7 | ASP | LEU | GLU |
sample_1: Domain Swapped GLPG, [U-100% 13C; U-100% 15N], 1 mM; NaH2PO4 25 mM; NaCl 150 mM; H2O 90%; D2O, [U-100% 2H], 10%
sample_conditions_1: ionic strength: 0.3 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | 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-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
| NCBI | ECs4267 |
| BMRB | 17720 |
| PDB | |
| DBJ | BAB37690 BAE77868 BAG79214 BAI27681 BAI32850 |
| EMBL | CAP77869 CAQ33744 CAR00366 CAR05025 CAR10074 |
| GB | AAG58528 AAN44906 AAN82639 AAP19275 AAT48182 |
| REF | NP_312294 NP_709199 WP_000541600 WP_000928708 WP_000928709 |
| SP | A1AGU7 A7ZSV4 A8A5N2 A8AQX4 B1IP42 |
| AlphaFold | A1AGU7 A7ZSV4 A8A5N2 A8AQX4 B1IP42 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks