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 34052

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34052
MolProbity Validation Chart

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Title: Solution structure of CsgF in DHPC micelles   PubMed: 29427517

Deposition date: 2016-10-10 Original release date: 2017-10-05

Authors: Spehr, J.; Schubeis, T.; Ahmed, M.; Ritter, C.

Citation: Schubeis, Tobias; Spehr, Johannes; Viereck, Janika; Kopping, Laura; Nagaraj, Madhu; Ahmed, Mumdooh; Ritter, Christiane. "Structural and functional characterization of the Curli adaptor protein CsgF."  FEBS Lett. 592, 1020-1029 (2018).

Assembly members:
entity_1, polymer, 127 residues, 13947.131 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 83333   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity_1: MAGTMTFQFRNPNFGGNPNN GAFLLNSAQAQNSYKDPSYN DDFGIETPSALDNFTQAIQS QILGGLLSNINTGKPGRMVT NDYIVDIANRDGQLQLNVTD RKTGQTSTIQVSGLQNNSTD FHHHHHH

Data sets:
Data typeCount
13C chemical shifts428
15N chemical shifts122
1H chemical shifts671

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 127 residues - 13947.131 Da.

1   METALAGLYTHRMETTHRPHEGLNPHEARG
2   ASNPROASNPHEGLYGLYASNPROASNASN
3   GLYALAPHELEULEUASNSERALAGLNALA
4   GLNASNSERTYRLYSASPPROSERTYRASN
5   ASPASPPHEGLYILEGLUTHRPROSERALA
6   LEUASPASNPHETHRGLNALAILEGLNSER
7   GLNILELEUGLYGLYLEULEUSERASNILE
8   ASNTHRGLYLYSPROGLYARGMETVALTHR
9   ASNASPTYRILEVALASPILEALAASNARG
10   ASPGLYGLNLEUGLNLEUASNVALTHRASP
11   ARGLYSTHRGLYGLNTHRSERTHRILEGLN
12   VALSERGLYLEUGLNASNASNSERTHRASP
13   PHEHISHISHISHISHISHIS

Samples:

sample_1: CsgF, [U-13C; U-15N], 400 uM; potassium phosphate 50 mM; DHPC 100 mM; NaN3 0.05%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 310 K

sample_conditions_2: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCC(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_2
2D 1H-13C HSQCsample_1isotropicsample_conditions_2
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_2
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_2
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_2
3D HCCH-TOCSYsample_1isotropicsample_conditions_2

Software:

CANDID, Herrmann, Guntert and Wuthrich - chemical shift assignment

CARA, Keller and Wuthrich - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

PROSA, Guntert - processing

NMR spectrometers:

  • Bruker AvanceIII 600 MHz

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