BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19053

Title: Solution structure of FimA wt   PubMed: 24184277

Deposition date: 2013-02-24 Original release date: 2013-11-11

Authors: Walczak, Michal; Puorger, Chasper; Glockshuber, Rudi; Wider, Gerhard

Citation: Walczak, Michal; Puorger, Chasper; Glockshuber, Rudi; Wider, Gerhard. "Intramolecular Donor Strand Complementation in the E. coli Type 1 Pilus Subunit FimA Explains the Existence of FimA Monomers As Off-Pathway Products of Pilus Assembly That Inhibit Host Cell Apoptosis."  J. Mol. Biol. 426, 542-549 (2014).

Assembly members:
FimA_wt, polymer, 159 residues, 15835.380 Da.

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

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

Entity Sequences (FASTA):
FimA_wt: AATTVNGGTVHFKGEVVNAA CAVDAGSVDQTVQLGQVRTA SLAQEGATSSAVGFNIQLND CDTNVASKAAVAFLGTAIDA GHTNVLALQSSAAGSATNVG VQILDRTGAALTLDGATFSS ETTLNNGTNTIPFQARYFAT GAATPGAANADATFKVQYQ

Data sets:
Data typeCount
1H chemical shifts668

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FimA wt1

Entities:

Entity 1, FimA wt 159 residues - 15835.380 Da.

1   ALAALATHRTHRVALASNGLYGLYTHRVAL
2   HISPHELYSGLYGLUVALVALASNALAALA
3   CYSALAVALASPALAGLYSERVALASPGLN
4   THRVALGLNLEUGLYGLNVALARGTHRALA
5   SERLEUALAGLNGLUGLYALATHRSERSER
6   ALAVALGLYPHEASNILEGLNLEUASNASP
7   CYSASPTHRASNVALALASERLYSALAALA
8   VALALAPHELEUGLYTHRALAILEASPALA
9   GLYHISTHRASNVALLEUALALEUGLNSER
10   SERALAALAGLYSERALATHRASNVALGLY
11   VALGLNILELEUASPARGTHRGLYALAALA
12   LEUTHRLEUASPGLYALATHRPHESERSER
13   GLUTHRTHRLEUASNASNGLYTHRASNTHR
14   ILEPROPHEGLNALAARGTYRPHEALATHR
15   GLYALAALATHRPROGLYALAALAASNALA
16   ASPALATHRPHELYSVALGLNTYRGLN

Samples:

sample_1: FimA_wt, [U-99% 13C; U-99% 15N], 2 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0.08 M; pH: 7; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY, Brunger, Adams, Clore, Gros, Nilges and Read, Goddard, Guntert, Mumenthaler and Wuthrich, Keller and Wuthrich - chemical shift assignment, refinement, structure solution

NMR spectrometers:

  • Bruker Avance 750 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 25334
PDB
DBJ BAE78307 BAJ46028
EMBL CAA25489 CAQ34662 CAR16032 CAS12169 CCJ47011
GB AAA24389 AAA97210 AAC77270 AAG35683 AAO84630
REF NP_418734 WP_000695553 WP_000695557 WP_000695559 WP_000695560
SP P04128