BMRB Entry 52035

Title:
FapA
Deposition date:
2023-07-13
Original release date:
2023-07-18
Authors:
Byeon, Chang-Hyeock; Akbey, Umit
Citation:

Citation: Byeon, Chang-Hyeock; Akbey, Umit. "Solution-state NMR assignment and secondary structure analysis of the monomeric Pseudomonas biofilm-forming functional amyloid accessory protein FapA"  Biomol. NMR Assign. 17, 275-280 (2023).
PubMed: 37798606

Assembly members:

Assembly members:
entity_1, polymer, 128 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Pseudomonas aeruginosa   Taxonomy ID: 287   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudomonas aeruginosa

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET32

Data sets:
Data typeCount
13C chemical shifts231
15N chemical shifts120
1H chemical shifts120

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FapA1

Entities:

Entity 1, FapA 128 residues - Formula weight is not available

FapA is a 152 amino acid containing protein. The first 28 amino acid is from the signal peptide that is cleaved in the functional form. In the construct we prepared for NMR analysis, there are four non-native - additional amino acids in this sequence: The first three amino acids 'SGT' and the last 'W' are not natively present in FapA protein. The first three are cleave artifacts, and the last W is added for quantification. The first amino acid of the functional FapA is E(29) and the last amino acid is P(152)

1   SERGLYTHRGLUASPGLYILEILEVALTHR
2   GLYARGASNVALGLNGLYPHEMETVALGLY
3   ARGPROSERPHEGLYLYSASPPROTYRPRO
4   SERTHRALAASNALAASNPROSERGLNGLN
5   ILELEUARGALATHRGLYGLYGLULEUSER
6   ASPASNASPPHEALAGLYVALSERSERGLY
7   SERTHRILETHRARGALAILELEUPROASN
8   GLYASPLEUPROGLYLEUSERASNTHRLEU
9   GLYASNASNSERALAGLYLEUGLYALAGLY
10   ALAALAALAGLYHISALASERGLYASNSER
11   LEUGLYGLYGLNILESERGLYSERILEGLU
12   ARGGLYLEUALAPROLEUASNASNILEGLY
13   ALAMETMETGLYVALGLNPROTRP

Samples:

sample_1: FapA, [U-13C; U-15N], 200 uM; DSS 1 mM; D2O, [U-99% 2H], 10%; sodium phosphate 20 mM

sample_conditions_1: pH: 7.8; pressure: 1 atm; temperature: 274 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1

Software:

CcpNMR v3.1 - chemical shift assignment

TOPSPIN v3.1 - collection, processing

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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