BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16628

Title: Sequence-specific 1H, 13C and 15N resonance assignments of the nucleotide-free wildtype cyclic nucleotide binding domain from a cyclic nucleotide-activated K+ channel   PubMed: 20449776

Deposition date: 2009-12-06 Original release date: 2010-07-19

Authors: Schuenke, Sven; Lecher, Justin; Stoldt, Matthias; Willbold, Dieter

Citation: Schunke, Sven; Lecher, Justin; Stoldt, Matthias; Kaupp, U. Benjamin; Willbold, Dieter. "Resonance assignments of the nucleotide-free wildtype MloK1 cyclic nucleotide-binding domain."  Biomol. NMR Assignments 4, 147-150 (2010).

Assembly members:
MloK1_CNBD, polymer, 142 residues, Formula weight is not available

Natural source:   Common Name: Mesorhizobium loti   Taxonomy ID: 381   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mesorhizobium loti

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
MloK1_CNBD: GSQEVRRGDFVRNWQLVAAV PLFQKLGPAVLVEIVRALRA RTVPAGAVICRIGEPGDRMF FVVEGSVSVATPNPVELGPG AFFGEMALISGEPRSATVSA ATTVSLLSLHSADFQMLCSS SPEIAEIFRKTALERRGAAA SA

Data sets:
Data typeCount
13C chemical shifts540
15N chemical shifts134
1H chemical shifts930

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MloK1 CNBD monomer1

Entities:

Entity 1, MloK1 CNBD monomer 142 residues - Formula weight is not available

Residues 214-215 represent the cleavage hang over of an affinity GST-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

Samples:

sample_1: MloK1 CNBD, [U-15N], 0.5 mM; TRIS, [U-99% 2H], 10 mM; sodium chloride 100 mM; sodium azide 0.02%; D2O, [U-100% 2H], 5%; H2O 95%; EDTA 200 uM

sample_2: MloK1 CNBD, [U-13C; U-15N], 0.5 mM; TRIS, [U-99% 2H], 10 mM; sodium chloride 100 mM; sodium azide 0.02%; D2O, [U-100% 2H], 5%; H2O 95%; EDTA 200 uM

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_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

VNMRJ, Varian - collection

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

CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker INOVA 800 MHz
  • Bruker INOVA 600 MHz

Related Database Links:

BMRB 15249 18024
PDB
DBJ BAB50178
REF WP_010911524 WP_032931689
SP Q98GN8

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