BMRB Entry 15249

Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15249

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Title:
Sequence-Specific 1H, 13C and 15N Resonance Assignments of the Cyclic Nucleotide Binding Domain from a Cyclic Nucleotide-Gated Potassium Channel in Complex with cAMP
Deposition date:
2007-05-15
Original release date:
2007-09-17
Authors:
Schunke, Sven; Stoldt, Matthias; Willbold, Dieter
Citation:

Citation: Schunke, Sven; Novak, Kerstin; Stoldt, Matthias; Kaupp, U. Benjamin; Willbold, Dieter. "Resonance assignment of the cyclic nucleotide binding domain from a cyclic nucleotide-gated K(+) channel in complex with cAMP"  Biomol. NMR Assignments 1, 179-181 (2007).
PubMed: 19636859

Assembly members:

Assembly members:
MlotiCNBDc, polymer, 142 residues, 14968.2 Da.
CMP, non-polymer, 329.206 Da.

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: pGEX-2T

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MlotiCNBDc: GSQEVRRGDFVRNWQLVAAV PLFQKLGPAVLVEIVRALRA RTVPAGAVICRIGEPGDRMF FVVEGSVSVATPNPVELGPG AFFGEMALISGEPRSATVSA ATTVSLLSLHSADFQMLCSS SPEIAEIFRKTALERRGAAA SA

Data sets:
Data typeCount
13C chemical shifts589
15N chemical shifts139
1H chemical shifts956

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MLoti Cyclic nucleotide binding domain1
2cAMP2

Entities:

Entity 1, MLoti Cyclic nucleotide binding domain 142 residues - 14968.2 Da.

Residues 216-355 represent the cAMP-binding domain of a cyclic nucleotide-gated potassium channel from the bacterium M. loti (residues 214-215 represent a non-native affinity tag).

1   GLYSERGLNGLUVALARGARGGLYASPPHE
2   VALARGASNTRPGLNLEUVALALAALAVAL
3   PROLEUPHEGLNLYSLEUGLYPROALAVAL
4   LEUVALGLUILEVALARGALALEUARGALA
5   ARGTHRVALPROALAGLYALAVALILECYS
6   ARGILEGLYGLUPROGLYASPARGMETPHE
7   PHEVALVALGLUGLYSERVALSERVALALA
8   THRPROASNPROVALGLULEUGLYPROGLY
9   ALAPHEPHEGLYGLUMETALALEUILESER
10   GLYGLUPROARGSERALATHRVALSERALA
11   ALATHRTHRVALSERLEULEUSERLEUHIS
12   SERALAASPPHEGLNMETLEUCYSSERSER
13   SERPROGLUILEALAGLUILEPHEARGLYS
14   THRALALEUGLUARGARGGLYALAALAALA
15   SERALA

Entity 2, cAMP - C10 H12 N5 O6 P - 329.206 Da.

1   CMP

Samples:

sample_1: MlotiCNBDc, [U-13C; U-15N], 0.5 mM; potassium phosphate 10 mM; potassium chloride 100 mM; cAMP 0.5 mM; sodium azide 0.02 % v/v; D2O, [U-2H], 5 % v/v; H2O 95 % v/v

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Varian Unity_INOVA 800 MHz

Related Database Links:

BMRB 16628 18024
PDB
DBJ BAB50178
REF WP_010911524 WP_032931689
SP Q98GN8
AlphaFold Q98GN8

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