BMRB Entry 19713

Title:
Solution Structure of Domain-Swapped GLPG
Deposition date:
2013-12-31
Original release date:
2014-11-10
Authors:
Ghasriani, Houman; Kwok, Jason; Sherrat, Allison; Goto, Natalie
Citation:

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:

Assembly members:
Domain_Swapped_GLPG, polymer, 63 residues, 7156.092 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PET 30A +

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Domain_Swapped_GLPG: MLMITSFANPRVAQAFVDYM ATQGVILTIQQHNQSDVWLA DESQAERVRAELARFLENPA DLE

Data sets:
Data typeCount
13C chemical shifts193
15N chemical shifts69
1H chemical shifts429

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Domain_Swapped_GLPG_11
2Domain_Swapped_GLPG_21

Entities:

Entity 1, Domain_Swapped_GLPG_1 63 residues - 7156.092 Da.

1   METLEUMETILETHRSERPHEALAASNPRO
2   ARGVALALAGLNALAPHEVALASPTYRMET
3   ALATHRGLNGLYVALILELEUTHRILEGLN
4   GLNHISASNGLNSERASPVALTRPLEUALA
5   ASPGLUSERGLNALAGLUARGVALARGALA
6   GLULEUALAARGPHELEUGLUASNPROALA
7   ASPLEUGLU

Samples:

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 800 MHz

Related Database Links:

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 A8A5N2 A8AQX4 B1IP42 A7ZSV4

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks