BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 30765

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR30765

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Title: Structural characterization of the type III secretion system pilotin-secretin complex InvH-InvG by NMR spectroscopy   PubMed: 32877645

Deposition date: 2020-06-15 Original release date: 2020-09-14

Authors: Majewski, D.; Okon, M.; Heinkel, F.; Robb, C.; Vuckovic, M.; McIntosh, L.; Strynadka, N.

Citation: Majewski, D.; Okon, M.; Heinkel, F.; Robb, C.; Vuckovic, M.; McIntosh, L.; Strynadka, N.. "Characterization of the pilotin-secretin complex from the Salmonella enterica type III secretion system using hybrid structural methods"  Structure ., .-. (2020).

Assembly members:
entity_1, polymer, 82 residues, 9453.652 Da.
entity_2, polymer, 47 residues, 5248.818 Da.

Natural source:   Common Name: Salmonella enterica   Taxonomy ID: 99287   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Salmonella enterica

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

Entity Sequences (FASTA):
entity_1: GSHMDNSASKNSAISSSIFC EKYKQTKEQALTFFQEHPQY MRSKEDEEQLMTEFKKVLLE PGSKNLSIYQTLLAAHERLQ AL
entity_2: GSHMDPLTPDASESVNNILK QSGAWSGDDKLQKWVRVYLD RGQEAIK

Data typeCount
13C chemical shifts551
15N chemical shifts134
1H chemical shifts876

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 82 residues - 9453.652 Da.

1   GLYSERHISMETASPASNSERALASERLYS
2   ASNSERALAILESERSERSERILEPHECYS
3   GLULYSTYRLYSGLNTHRLYSGLUGLNALA
4   LEUTHRPHEPHEGLNGLUHISPROGLNTYR
5   METARGSERLYSGLUASPGLUGLUGLNLEU
6   METTHRGLUPHELYSLYSVALLEULEUGLU
7   PROGLYSERLYSASNLEUSERILETYRGLN
8   THRLEULEUALAALAHISGLUARGLEUGLN
9   ALALEU

Entity 2, unit_2 47 residues - 5248.818 Da.

1   GLYSERHISMETASPPROLEUTHRPROASP
2   ALASERGLUSERVALASNASNILELEULYS
3   GLNSERGLYALATRPSERGLYASPASPLYS
4   LEUGLNLYSTRPVALARGVALTYRLEUASP
5   ARGGLYGLNGLUALAILELYS

Samples:

sample_1: entity_1, [U-13C; U-15N], 0.5 mM; entity_2, [U-13C; U-15N], 0.5 mM; MOPS 20 mM; sodium chloride 150 mM; TCEP 0.2 mM; D2O 10 % v/v

sample_2: entity_1, [U-13C; U-15N], 0.5 mM; entity_2, [U-13C; U-15N], 0.5 mM; MOPS 20 mM; sodium chloride 150 mM; TCEP 0.2 mM; D2O 10 % v/v

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCC(CO)NH-TOCSYsample_1isotropicsample_conditions_1
3D hbCBcgcCHsample_1isotropicsample_conditions_1
3D hbCBcgcdceHEsample_1isotropicsample_conditions_1
3D hbCBcgcdHDsample_1isotropicsample_conditions_1
3D HBHA(CBCACO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESY filtered-editedsample_1isotropicsample_conditions_1
3D 1H-13C NOESY filtered-editedsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D hbCBcgcCHsample_2isotropicsample_conditions_1
3D hbCBcgcdceHEsample_2isotropicsample_conditions_1
3D hbCBcgcdHDsample_2isotropicsample_conditions_1
3D HBHA(CBCACO)NHsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HCC(CO)NH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESY filtered-editedsample_2isotropicsample_conditions_1
3D 1H-13C NOESY filtered-editedsample_2isotropicsample_conditions_1

Software:

CYANA v3.98.13, Guntert P., Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

NMRFAM-SPARKY, Lee W, Tonelli M, Markley JL - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE 500 MHz
  • Bruker AVANCE 850 MHz

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