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 6947

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6947

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Title: Backbone 1H, 13C, and 15N Chemical Shift assignments for dimeric E.coli Ferric Uptake Regulator (Fur)   PubMed: 16690618

Deposition date: 2006-01-24 Original release date: 2007-02-06

Authors: Pecqueur, Ludovic; D'Autreaux, Benoit; Brutscher, Bernhard; Michaud-Soret, Isabelle; Bersch, Beate

Citation: Pecqueur, Ludovic; D'Autreaux, Benoit; Dupuy, Jerome; Nicolet, Yvain; Jacquamet, Lilian; Brutscher, Bernhard; Michaud-Soret, Isabelle; Bersch, Beate. "Structural changes of E. coli Ferric uptake regulator during metal-dependent dimerization and activation explored by NMR and X-ray crystallography"  J. Biol. Chem. 281, 21286-21295 (2006).

Assembly members:
Fur, polymer, 147 residues, 17000 Da.
ZN, non-polymer, 65.409 Da.

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

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
Fur: TDNNTALKKAGLKVTLPRLK ILEVLQEPDNHHVSAEDLYK RLIDMGEEIGLATVYRVLNQ FDDAGIVTRHNFEGGKSVFE LTQQHHHDHLICLDCGKVIE FSDDSIEARQREIAAKHGIR LTNHSLYLYGHCAEGDCRED EHAHEGK

Data sets:
Data typeCount
13C chemical shifts517
15N chemical shifts135
1H chemical shifts518

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Fur subunit 11
2Fur subunit 21
3ZINC (II) ION, 12
4ZINC (II) ION, 22

Entities:

Entity 1, Fur subunit 1 147 residues - 17000 Da.

sequence numbering corresponds to the biological unit after Met1 cleavage

1   THRASPASNASNTHRALALEULYSLYSALA
2   GLYLEULYSVALTHRLEUPROARGLEULYS
3   ILELEUGLUVALLEUGLNGLUPROASPASN
4   HISHISVALSERALAGLUASPLEUTYRLYS
5   ARGLEUILEASPMETGLYGLUGLUILEGLY
6   LEUALATHRVALTYRARGVALLEUASNGLN
7   PHEASPASPALAGLYILEVALTHRARGHIS
8   ASNPHEGLUGLYGLYLYSSERVALPHEGLU
9   LEUTHRGLNGLNHISHISHISASPHISLEU
10   ILECYSLEUASPCYSGLYLYSVALILEGLU
11   PHESERASPASPSERILEGLUALAARGGLN
12   ARGGLUILEALAALALYSHISGLYILEARG
13   LEUTHRASNHISSERLEUTYRLEUTYRGLY
14   HISCYSALAGLUGLYASPCYSARGGLUASP
15   GLUHISALAHISGLUGLYLYS

Entity 2, ZINC (II) ION, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: FurD, [U-46% 2H; U-97% 15N; U-13C], 2.6 ± 0.1 mM; MOPS 100 mM; KCl 500 mM; DTT 10 mM; D20 7%

sample_2: FurD, [U-97% 15N], 2.1 ± 0.1 mM; MOPS 100 mM; KCl 500 mM; DTT 10 mM; D20 7%

sample_3: FurD, [U-97% 15N; U-13C], 1.5 ± 0.1 mM; MOPS 100 mM; KCl 500 mM; DTT 10 mM; D20 7%

sample_4: FurD, [U-97% 15N; U-13C], 1.5 ± 0.1 mM; MOPS 100 mM; KCl 500 mM; DTT 10 mM; D20 100%

conditions_1: pH: 7.5; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H15N_HSQCsample_1not availableconditions_1
1H15N13C_MQ_COHNCAsample_1not availableconditions_1
1H15N13C_MQ_HNCOCAsample_1not availableconditions_1
1H15N13C_HNCACOsample_1not availableconditions_1
1H15N13C_HN(CA)CBsample_1not availableconditions_1
1H15N13C_HN(COCA)CBsample_1not availableconditions_1
HNCOsample_1not availableconditions_1
HCCH-TOCSYsample_4not availableconditions_1
(H)CCH-TOCSYsample_4not availableconditions_1
(H)CCONH-TOCSYsample_3not availableconditions_1
H(C)CONH-TOCSYsample_3not availableconditions_1

Software:

FELIX v2000, Accelrys -

NMR spectrometers:

  • Varian Inova 600 MHz
  • Varian Inova 800 MHz

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