BMRB Entry 18392

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the C-terminal Domain of E. coli Enzyme I
Deposition date:
2012-04-12
Original release date:
2012-09-14
Authors:
Venditti, Vincenzo; Clore, G. Marius
Citation:

Citation: Venditti, Vincenzo; Clore, G. Marius. "Conformational Selection and Substrate Binding Regulate the Monomer/Dimer Equilibrium of the C-terminal domain of Escherichia coli Enzyme I."  J. Biol. Chem. 287, 26989-26998 (2012).
PubMed: 22722931

Assembly members:

Assembly members:
EIC, polymer, 316 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: pET11a

Data sets:
Data typeCount
13C chemical shifts810
15N chemical shifts266
1H chemical shifts266

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EIC subunit 11
2EIC subunit 21

Entities:

Entity 1, EIC subunit 1 316 residues - Formula weight is not available

1   METALAILETHRLEUASPGLYHISGLNVAL
2   GLUVALCYSALAASNILEGLYTHRVALARG
3   ASPVALGLUGLYALAGLUARGASNGLYALA
4   GLUGLYVALGLYLEUTYRARGTHRGLUPHE
5   LEUPHEMETASPARGASPALALEUPROTHR
6   GLUGLUGLUGLNPHEALAALATYRLYSALA
7   VALALAGLUALACYSGLYSERGLNALAVAL
8   ILEVALARGTHRMETASPILEGLYGLYASP
9   LYSGLULEUPROTYRMETASNPHEPROLYS
10   GLUGLUASNPROPHELEUGLYTRPARGALA
11   ILEARGILEALAMETASPARGLYSGLUILE
12   LEUARGASPGLNLEUARGALAILELEUARG
13   ALASERALAPHEGLYLYSLEUARGILEMET
14   PHEPROMETILEILESERVALGLUGLUVAL
15   ARGALALEUARGLYSGLUILEGLUILETYR
16   LYSGLNGLULEUARGASPGLUGLYLYSALA
17   PHEASPGLUSERILEGLUILEGLYVALMET
18   VALGLUTHRPROALAALAALATHRILEALA
19   ARGHISLEUALALYSGLUVALASPPHEPHE
20   SERILEGLYTHRASNASPLEUTHRGLNTYR
21   THRLEUALAVALASPARGGLYASNASPMET
22   ILESERHISLEUTYRGLNPROMETSERPRO
23   SERVALLEUASNLEUILELYSGLNVALILE
24   ASPALASERHISALAGLUGLYLYSTRPTHR
25   GLYMETCYSGLYGLULEUALAGLYASPGLU
26   ARGALATHRLEULEULEULEUGLYMETGLY
27   LEUASPGLUPHESERMETSERALAILESER
28   ILEPROARGILELYSLYSILEILEARGASN
29   THRASNPHEGLUASPALALYSVALLEUALA
30   GLUGLNALALEUALAGLNPROTHRTHRASP
31   GLULEUMETTHRLEUVALASNLYSPHEILE
32   GLUGLULYSTHRILECYS

Samples:

sample_1: EIC, [U-13C; U-15N; U-2H], 0.3-0.4 mM; sodium chloride 100 mM; TRIS 20 mM; magnesium chloride 4 mM; EDTA 1 mM

sample_conditions_1: pH: 7.4; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 25731
PDB
DBJ BAA16290 BAB36711 BAG78231 BAH64557 BAI26669
EMBL CAP76888 CAQ32794 CAQ88296 CAQ99314 CAR03878
GB AAA24385 AAA24441 AAA27060 AAC75469 AAG57535
REF NP_311315 NP_416911 NP_461367 NP_708271 WP_000112669
SP P08839 P0A249 P0A250
AlphaFold P08839 P0A249 P0A250

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