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 51793

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51793

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Title: FapC Full-Length   PubMed: 37162737

Deposition date: 2023-01-22 Original release date: 2023-01-27

Authors: Byeon, Chang-Hyeock; Wang, Pang; Byeon, In-Ja; akbey, umit

Citation: Byeon, Chang-Hyeock; Wang, Pang; Byeon, In-Ja; Akbey, Umit. "Solution-state NMR assignment and secondary structure propensity of the full length and minimalistic-truncated prefibrillar monomeric form of biofilm forming functional amyloid FapC from Pseudomonas aeruginosa"  Biomol. NMR Assign. 17, 159-165 (2023).

Assembly members:
entity_1, polymer, 235 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):
entity_1: MGPAEKWKPTPAPTGTVAAA VTDTQVSKDNKFDDTKTLNN AGANGSLSNSKGNLGANIAA GSGNQQDNAAAITSSAGDAA TVFAVADIYQESKDNKFTNK GTQNNALLNNSANNSSGNVG VNVAAGQGNQQKNNLAIVTA DGKNVAAASNTEQVSLDNHF LNEASSKHSYKPQYVVNNAG LLNSANNASGNIGVNVAAGA GNQQSNTLTLGSGCTVCAAG TGSKLAFLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts417
15N chemical shifts198
1H chemical shifts764

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FapC Full-Length1

Entities:

Entity 1, FapC Full-Length 235 residues - Formula weight is not available

Residue 1 is a nonnative Methionine. The last 8 residues are nonnative and due to the His-tag. The original aminoacids and the numbering in the FapC FapC is as: G25,P26,A27,...

1   METGLYPROALAGLULYSTRPLYSPROTHR
2   PROALAPROTHRGLYTHRVALALAALAALA
3   VALTHRASPTHRGLNVALSERLYSASPASN
4   LYSPHEASPASPTHRLYSTHRLEUASNASN
5   ALAGLYALAASNGLYSERLEUSERASNSER
6   LYSGLYASNLEUGLYALAASNILEALAALA
7   GLYSERGLYASNGLNGLNASPASNALAALA
8   ALAILETHRSERSERALAGLYASPALAALA
9   THRVALPHEALAVALALAASPILETYRGLN
10   GLUSERLYSASPASNLYSPHETHRASNLYS
11   GLYTHRGLNASNASNALALEULEUASNASN
12   SERALAASNASNSERSERGLYASNVALGLY
13   VALASNVALALAALAGLYGLNGLYASNGLN
14   GLNLYSASNASNLEUALAILEVALTHRALA
15   ASPGLYLYSASNVALALAALAALASERASN
16   THRGLUGLNVALSERLEUASPASNHISPHE
17   LEUASNGLUALASERSERLYSHISSERTYR
18   LYSPROGLNTYRVALVALASNASNALAGLY
19   LEULEUASNSERALAASNASNALASERGLY
20   ASNILEGLYVALASNVALALAALAGLYALA
21   GLYASNGLNGLNSERASNTHRLEUTHRLEU
22   GLYSERGLYCYSTHRVALCYSALAALAGLY
23   THRGLYSERLYSLEUALAPHELEUGLUHIS
24   HISHISHISHISHIS

Samples:

sample_1: FapC Full-Lentgh, [U-13C; U-15N], 0.3 mM; DSS, [U-99% 2H], 1 mM; D2O, [U-99% 2H], 10%; DTT 30 mM; sodium phosphate 50 mM; sodium azide 0.02%

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 274 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 HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

CcpNMR v3.1 - chemical shift assignment

TOPSPIN v3 - collection

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 900 MHz

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