BMRB Entry 6779

Title:
Solution Structure of the type 1 pilus assembly platform FimD(25-125)
Deposition date:
2005-08-17
Original release date:
2005-10-18
Authors:
Nishiyama, M.; Horst, R.; Herrmann, R.; Vetsch, M.; Bettendorff, P.; Ignatov, O.; Grutter, M.; Wuthrich, K.; Glockshuber, R.; Capitani, G.
Citation:

Citation: Nishiyama, M.; Horst, R.; Herrmann, R.; Vetsch, M.; Bettendorff, P.; Ignatov, O.; Grutter, M.; Wuthrich, K.; Glockshuber, R.; Capitani, G.. "Structural basis of chaperone-subunit complex recognition by type 1 pilus assembly platform FimD"  EMBO J. 24, 2075-2086 (2005).
PubMed: 15920478

Assembly members:

Assembly members:
FimD, polymer, 101 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology

Data sets:
Data typeCount
1H chemical shifts657
13C chemical shifts310
15N chemical shifts107

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Outer membrane usher protein FimD1

Entities:

Entity 1, Outer membrane usher protein FimD 101 residues - Formula weight is not available

1   GLYGLNGLULEUPROPROGLYTHRTYRARG
2   VALASPILETYRLEUASNASNGLYTYRMET
3   ALATHRARGASPVALTHRPHEASNTHRGLY
4   ASPSERGLUGLNGLYILEVALPROCYSLEU
5   THRARGALAGLNLEUALASERMETGLYLEU
6   ASNTHRALASERVALALAGLYMETASNLEU
7   LEUALAASPASPALACYSVALPROLEUTHR
8   THRMETVALGLNASPALATHRALAHISLEU
9   ASPVALGLYGLNGLNARGLEUASNLEUTHR
10   ILEPROGLNALAPHEMETSERASNARGALA
11   ARG

Samples:

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

sample_cond_1: pH: 7.0; temperature: 293 K; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYnot availablenot availablenot available
3D 13C-separated NOESYnot availablenot availablenot available

Software:

XWINNMR v3.5 - collection

ATHNOS-CANDID - structure solution, refinement

NMR spectrometers:

  • Bruker AVANCE 900 MHz

Related Database Links:

BMRB 6629
PDB
DBJ BAB38699 BAE78310 BAI28636 BAI33777 BAJ46031
EMBL CAQ34665 CAR16035 CCP96085 CCQ07908 CCW23202
GB AAA97213 AAC77273 AAG59499 AAY89700 ABF06193
REF NP_290933 NP_313303 NP_418737 WP_000120908 WP_000120909
SP P30130
AlphaFold P30130

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