BMRB Entry 26999

Title:
Adenylate kinase in Apo form
Deposition date:
2017-01-19
Original release date:
2019-07-30
Authors:
Rogne, Per; Wolf-Watz, Magnus
Citation:

Citation: Rogne, Per; Andersson, David; Grundstrom, Christin; Sauer-Eriksson, Elisabeth; Linusson, Anna; Wolf-Watz, Magnus. "Nucleation of an Activating Conformational Change by a Cation-pi Interaction"  Biochemistry 58, 3408-3412 (2019).
PubMed: 31339702

Assembly members:

Assembly members:
Wild_type, 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: pEAK91

Data sets:
Data typeCount
15N chemical shifts190
1H chemical shifts190

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AdK1

Entities:

Entity 1, AdK 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   GLUGLUTHRVALARGLYSARGLEUVALGLU
18   TYRHISGLNMETTHRALAPROLEUILEGLY
19   TYRTYRSERLYSGLUALAGLUALAGLYASN
20   THRLYSTYRALALYSVALASPGLYTHRLYS
21   PROVALALAGLUVALARGALAASPLEUGLU
22   LYSILELEUGLY

Samples:

ApoWT_sample: Wild type, [U-15N], 200 uM; MOPS 30 mM; NaCl 50 mM; TMSP 100 uM

sample_conditions_1: ionic strength: 80 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCApoWT_sampleisotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection

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

ANSIG, Kraulis - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AvanceIIIHD 850 MHz

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