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

Title: Solution structure of CsgF in DHPC micelles

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

Citation: Spehr, J.; Schubeis, T.. "Solution structure of the curli adaptor protein CsgF"  . ., .-..

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
  • Hide all

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

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