BMRB Entry 36516

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36516
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

Title:
Solution structure of the periplasmic domain of RsgI6 from Clostridium thermocellum
Deposition date:
2022-11-08
Original release date:
2023-05-30
Authors:
Chen, C.; Feng, Y.
Citation:

Citation: Chen, C.; Feng, Y.. "Essential autoproteolysis of bacterial anti-sigma factor RsgI for signal transmembrane transduction"  .

Assembly members:

Assembly members:
Anti-sigma factor, polymer, 10 residues, 1158.325 Da.
Anti-sigma factor, polymer, 166 residues, 18660.010 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 637887   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Acetivibrio thermocellus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Anti-sigma factor: MYAYVGIDIN
Anti-sigma factor: PSIELWINYNNKIAEAKALN GDAETVLEGLELKEKTVAEA VNEIVQKSMELGFISREKEN IILISTACDLKAGEGSENKD VQNKIGQLFDDVNKAVSDLK NSGITTRILNLTLEERESSK EENISMGRYAVYLKAKEQNV NLTIDEIKDADLLELIAKLE HHHHHH

Data sets:
Data typeCount
13C chemical shifts768
15N chemical shifts192
1H chemical shifts1256

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22

Entities:

Entity 1, unit_1 10 residues - 1158.325 Da.

1   METTYRALATYRVALGLYILEASPILEASN

Entity 2, unit_2 166 residues - 18660.010 Da.

1   PROSERILEGLULEUTRPILEASNTYRASN
2   ASNLYSILEALAGLUALALYSALALEUASN
3   GLYASPALAGLUTHRVALLEUGLUGLYLEU
4   GLULEULYSGLULYSTHRVALALAGLUALA
5   VALASNGLUILEVALGLNLYSSERMETGLU
6   LEUGLYPHEILESERARGGLULYSGLUASN
7   ILEILELEUILESERTHRALACYSASPLEU
8   LYSALAGLYGLUGLYSERGLUASNLYSASP
9   VALGLNASNLYSILEGLYGLNLEUPHEASP
10   ASPVALASNLYSALAVALSERASPLEULYS
11   ASNSERGLYILETHRTHRARGILELEUASN
12   LEUTHRLEUGLUGLUARGGLUSERSERLYS
13   GLUGLUASNILESERMETGLYARGTYRALA
14   VALTYRLEULYSALALYSGLUGLNASNVAL
15   ASNLEUTHRILEASPGLUILELYSASPALA
16   ASPLEULEUGLULEUILEALALYSLEUGLU
17   HISHISHISHISHISHIS

Samples:

sample_1: DSS 0.02 % w/v; RsgI6-PD, [U-100% 13C; U-100% 15N], 1 mM; sodium chloride 150 mM; sodium phosphate 50 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 200 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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