BMRB Entry 15032

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15032
MolProbity Validation Chart

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Title:
Chemical shift assignments of the type 1 pilus subunit FimF
Deposition date:
2006-11-15
Original release date:
2007-05-09
Authors:
Gossert, Alvar; Hiller, Sebastian; Fiorito, Francesco; Wuthrich, Kurt
Citation:

Citation: Gossert, Alvar; Hiller, Sebastian; Fiorito, Francesco; Wuthrich, Kurt. "NMR assignment of the E. coli type 1 pilus protein FimF."  J. Biomol. NMR 38, 195-195 (2007).
PubMed: 17417715

Assembly members:

Assembly members:
FimF, polymer, 179 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FimF: MADSTITIRGYVRDNGCSVA AESTNFTVDLMENAAKQFNN IGATTPVVPFRILLSPCGNA VSAVKVGFTGVADSHNANLL ALENTVSAASGLGIQLLNEQ QNQIPLNAPSSALSWTTLTP GKPNTLNFYARLMATQVPVT AGHINATATFTLEYQDNHHH HHHKQADSTITIRGYVRDN

Data sets:
Data typeCount
13C chemical shifts675
15N chemical shifts192
1H chemical shifts1152

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1FimF1

Entities:

Entity 1, FimF 179 residues - Formula weight is not available

Residue MET 0 respresents an artirfact from cyoplasmic expression

1   METALAASPSERTHRILETHRILEARGGLY
2   TYRVALARGASPASNGLYCYSSERVALALA
3   ALAGLUSERTHRASNPHETHRVALASPLEU
4   METGLUASNALAALALYSGLNPHEASNASN
5   ILEGLYALATHRTHRPROVALVALPROPHE
6   ARGILELEULEUSERPROCYSGLYASNALA
7   VALSERALAVALLYSVALGLYPHETHRGLY
8   VALALAASPSERHISASNALAASNLEULEU
9   ALALEUGLUASNTHRVALSERALAALASER
10   GLYLEUGLYILEGLNLEULEUASNGLUGLN
11   GLNASNGLNILEPROLEUASNALAPROSER
12   SERALALEUSERTRPTHRTHRLEUTHRPRO
13   GLYLYSPROASNTHRLEUASNPHETYRALA
14   ARGLEUMETALATHRGLNVALPROVALTHR
15   ALAGLYHISILEASNALATHRALATHRPHE
16   THRLEUGLUTYRGLNASPASNHISHISHIS
17   HISHISHISLYSGLNALAASPSERTHRILE
18   THRILEARGGLYTYRVALARGASPASN

Samples:

sample_1: FimF, [U-99% 13C; U-99% 15N], 1.4 mM; sodium phosphate 25 mM; sodium chloride 100 mM; sodium azide 0.05%; D2O 5%; H2O 95%

sample_conditions_1: pH: 6.8; temperature: 310.1 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
4D APSY-HNCOCAsample_1isotropicsample_conditions_1
4D APSY-COHNCAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

CARA v1.5.5, Rochus Keller - chemical shift assignment

NMR spectrometers:

  • Bruker DMX 750 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
DBJ BAB38700 BAE78311 BAG80115 BAI28637 BAI33778
EMBL CAA12421 CAH55782 CAP78799 CAQ34666 CAR01275
GB AAA97214 AAC77274 AAG24828 AAG59500 AAN45623
REF NP_313304 NP_418738 NP_709916 WP_001244818 WP_001244819
SP P08189
AlphaFold P08189

Download HSQC peak lists in one of the following formats:
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