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Biological Magnetic Resonance Data Bank


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BMRB Entry 36515

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36515
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Title: Solution structure of the periplasmic domain of the anti-sigma factor RsgI1 from Clostridium thermocellum

Deposition date: 2022-11-08 Original release date: 2023-05-30

Authors: Chen, C.; Feng, Y.

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

Assembly members:
Anti-sigma factor, polymer, 10 residues, 1190.390 Da.
Anti-sigma factor, polymer, 166 residues, 19081.623 Da.

Natural source:   Common Name: Acetivibrio thermocellus DSM 1313   Taxonomy ID: 637887   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Acetivibrio thermocellus

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

Entity Sequences (FASTA):
Anti-sigma factor: MYGYICVDIN
Anti-sigma factor: PSVELVIDETCRVLEVRPQN KDGEQLISGLELLDKNVEDV VYELINRSISFGFVKADDNR KIVLISGALNDKRNELKTKK ENDEAELTELLDNIKARVDR IDNIKVRTITATSRERKDAL KYGLSMGKYCLYLEAQELNG SITIDEVHDMSISDMIEKLE HHHHHH

Data sets:
Data typeCount
13C chemical shifts773
15N chemical shifts189
1H chemical shifts1261

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22

Entities:

Entity 1, unit_1 10 residues - 1190.390 Da.

1   METTYRGLYTYRILECYSVALASPILEASN

Entity 2, unit_2 166 residues - 19081.623 Da.

1   PROSERVALGLULEUVALILEASPGLUTHR
2   CYSARGVALLEUGLUVALARGPROGLNASN
3   LYSASPGLYGLUGLNLEUILESERGLYLEU
4   GLULEULEUASPLYSASNVALGLUASPVAL
5   VALTYRGLULEUILEASNARGSERILESER
6   PHEGLYPHEVALLYSALAASPASPASNARG
7   LYSILEVALLEUILESERGLYALALEUASN
8   ASPLYSARGASNGLULEULYSTHRLYSLYS
9   GLUASNASPGLUALAGLULEUTHRGLULEU
10   LEUASPASNILELYSALAARGVALASPARG
11   ILEASPASNILELYSVALARGTHRILETHR
12   ALATHRSERARGGLUARGLYSASPALALEU
13   LYSTYRGLYLEUSERMETGLYLYSTYRCYS
14   LEUTYRLEUGLUALAGLNGLULEUASNGLY
15   SERILETHRILEASPGLUVALHISASPMET
16   SERILESERASPMETILEGLULYSLEUGLU
17   HISHISHISHISHISHIS

Samples:

sample_1: DSS 0.02 % w/v; RsgI1-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 shifts
SPARKY: Backbone or all simulated shifts