BMRB Entry 18686

Title:
1H and 15N backbone resonance assignments of Escherichia coli Adenylate kinase: E170A
Deposition date:
2012-08-30
Original release date:
2012-10-18
Authors:
Aden, Jorgen; Verma, Abhinav; Schug, Alexander; Wolf-Watz, Magnus
Citation:

Citation: Aden, Jorgen; Verma, Abhinav; Schug, Alexander; Wolf-Watz, Magnus. "Modulation of a Pre-existing Conformational Equilibrium Tunes Adenylate Kinase Activity."  J. Am. Chem. Soc. 134, 16562-16570 (2012).
PubMed: 22963267

Assembly members:

Assembly members:
adenylate_kinase, polymer, 214 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

Data sets:
Data typeCount
15N chemical shifts189
1H chemical shifts189

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1E coli adenylate kinase: E170A1

Entities:

Entity 1, E coli adenylate kinase: E170A 214 residues - Formula weight is not available

1   METARGILEILELEULEUGLYALAPROGLY
2   ALAGLYLYSGLYTHRGLNALAGLNPHEILE
3   METGLULYSTYRGLYILEPROGLNILESER
4   THRGLYASPMETLEUARGALAALAVALLYS
5   SERGLYSERGLULEUGLYLYSGLNALALYS
6   ASPILEMETASPALAGLYLYSLEUVALTHR
7   ASPGLULEUVALILEALALEUVALLYSGLU
8   ARGILEALAGLNGLUASPCYSARGASNGLY
9   PHELEULEUASPGLYPHEPROARGTHRILE
10   PROGLNALAASPALAMETLYSGLUALAGLY
11   ILEASNVALASPTYRVALLEUGLUPHEASP
12   VALPROASPGLULEUILEVALASPARGILE
13   VALGLYARGARGVALHISALAPROSERGLY
14   ARGVALTYRHISVALLYSPHEASNPROPRO
15   LYSVALGLUGLYLYSASPASPVALTHRGLY
16   GLUGLULEUTHRTHRARGLYSASPASPGLN
17   GLUGLUTHRVALARGLYSARGLEUVALALA
18   TYRHISGLNMETTHRALAPROLEUILEGLY
19   TYRTYRSERLYSGLUALAGLUALAGLYASN
20   THRLYSTYRALALYSVALASPGLYTHRLYS
21   PROVALALAGLUVALARGALAASPLEUGLU
22   LYSILELEUGLY

Samples:

sample_1: adenylate kinase, [U-100% 15N], 1 mM

Sample_2: adenylate kinase, [U-100% 15N], 1 mM

sample_3: adenylate kinase, [U-100% 15N], 1 mM; TMAO 0.35 mM

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCSample_2isotropicsample_conditions_1
3D 1H-15N NOESYSample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

BMRB 18683 18685 18687 19089 19090 19091 19092 19093 25353 25357 25360 25361 25362 4152 4193 4350
PDB
DBJ BAA14303 BAB33950 BAE76253 BAG76023 BAI23848
EMBL CAA26840 CAF33430 CAF33431 CAF33432 CAF33433
GB AAA23461 AAB40228 AAC73576 AAG54823 AAM94352
REF NP_308554 NP_415007 NP_706367 WP_001220233 WP_001220235
SP A7ZIN4 A7ZXD2 B1IZC0 B1LJN2 B1XFR1
AlphaFold A7ZIN4 A7ZXD2 B1IZC0 B1LJN2 B1XFR1

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