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Biological Magnetic Resonance Data Bank


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BMRB Entry 34450

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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/BMR34450
MolProbity Validation Chart

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Title: Solution structure of RfaH C-terminal domain from Vibrio cholerae   PubMed: 36255050

Deposition date: 2019-11-13 Original release date: 2021-11-19

Authors: Zuber, P.; Schweimer, K.; Knauer, S.

Citation: Zuber, Philipp; Daviter, Tina; Heissmann, Ramona; Persau, Ulrike; Schweimer, Kristian; Knauer, Stefan. "Structural and thermodynamic analyses of the beta-to-alpha transformation in RfaH reveal principles of fold-switching proteins"  Elife 11, e76630-e76630 (2022).

Assembly members:
entity_1, polymer, 67 residues, 7438.494 Da.

Natural source:   Common Name: Vibrio cholerae   Taxonomy ID: 666   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Vibrio cholerae

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pETGb1a_vcrfaH-CTD

Entity Sequences (FASTA):
entity_1: GAMGEQLKHATKQLPEKGQT VRVARGQFAGIEAIYLEPDG DTRSIMLVKMISQQVPMSIE NTDWEVT

Data sets:
Data typeCount
13C chemical shifts296
15N chemical shifts68
1H chemical shifts467

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 67 residues - 7438.494 Da.

1   GLYALAMETGLYGLUGLNLEULYSHISALA
2   THRLYSGLNLEUPROGLULYSGLYGLNTHR
3   VALARGVALALAARGGLYGLNPHEALAGLY
4   ILEGLUALAILETYRLEUGLUPROASPGLY
5   ASPTHRARGSERILEMETLEUVALLYSMET
6   ILESERGLNGLNVALPROMETSERILEGLU
7   ASNTHRASPTRPGLUVALTHR

Samples:

sample_1: Vibrio cholerae RfaH C-terminal domain, [U-99% 13C; U-99% 15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 100 mM

sample_2: Vibrio cholerae RfaH C-terminal domain, [U-99% 13C; U-99% 15N], 0.5 mM; potassium phosphate 10 mM; potassium chloride 50 mM

sample_conditions_1: ionic strength: 136 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 98 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C ctHSQC aliphaticsample_2isotropicsample_conditions_2
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_2
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_2isotropicsample_conditions_2
3D HBHA(CO)NHsample_2isotropicsample_conditions_2
3D CACOsample_2isotropicsample_conditions_2
3D CONsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_2isotropicsample_conditions_2
3D C(CO)NHsample_1isotropicsample_conditions_1
3D long range HNCOsample_2isotropicsample_conditions_2
13CO spinecho difference 13C ctHSQCsample_2isotropicsample_conditions_2
15N spinecho difference 13C ctHSQCsample_2isotropicsample_conditions_2

Software:

TopSpin vv3.5 pl5, Bruker Biospin - collection

NMRViewJ vv9.2.0-b2, Johnson, One Moon Scientific - chemical shift assignment, data analysis

NMRViewJ, Johnson, One Moon Scientific - peak picking

X-PLOR NIH vv1.2.1, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

  • Bruker AVANCE 600 MHz
  • Bruker AVANCE 700 MHz
  • Bruker Ascend Aeon 900 MHz

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