BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 17029

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17029

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Title: 1H, 15N and 13C assignments for the potential GTPase binding domain of dictyostelium discoideum Fomin C   PubMed: 21846933

Deposition date: 2010-06-30 Original release date: 2011-10-28

Authors: Dames, Sonja; Schoenichen, Andre; Stephan, Grzesiek; Geyer, Matthias

Citation: Dames, Sonja; Junemann, Alexander; Sass, Hans; Schonichen, Andre; Stopschinski, Barbara; Grzesiek, Stephan; Faix, Jan; Geyer, Matthias. "Structure, Dynamics, Lipid Binding, and Physiological Relevance of the Putative GTPase-binding Domain of Dictyostelium Formin C."  J. Biol. Chem. 286, 36907-36920 (2011).

Assembly members:
formin_C, polymer, 107 residues, 12057.7 Da.

Natural source:   Common Name: Dictyostelium discoideum   Taxonomy ID: 44689   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Dictyostelium discoideum

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

Entity Sequences (FASTA):
formin_C: GAHMGGSMKIRVELINGNEH RTSSTPQQPQQNPSVSHIFD GETAVKDHIKVLLTHFKIPV DKVSSYALQNPFTLAYVEDS FLTPERLVEAEKSYFILRMK PHAIADR

Data sets:
Data typeCount
13C chemical shifts482
15N chemical shifts111
1H chemical shifts782

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1formin C1

Entities:

Entity 1, formin C 107 residues - 12057.7 Da.

1   GLYALAHISMETGLYGLYSERMETLYSILE
2   ARGVALGLULEUILEASNGLYASNGLUHIS
3   ARGTHRSERSERTHRPROGLNGLNPROGLN
4   GLNASNPROSERVALSERHISILEPHEASP
5   GLYGLUTHRALAVALLYSASPHISILELYS
6   VALLEULEUTHRHISPHELYSILEPROVAL
7   ASPLYSVALSERSERTYRALALEUGLNASN
8   PROPHETHRLEUALATYRVALGLUASPSER
9   PHELEUTHRPROGLUARGLEUVALGLUALA
10   GLULYSSERTYRPHEILELEUARGMETLYS
11   PROHISALAILEALAASPARG

Samples:

sample_1: forC/ A, [U-100% 15N], 1.0 mM; potassium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.2%

sample_2: forC/ A, [U-100% 13C; U-100% 15N], 0.8 mM; potassium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.2%

sample_3: forC/ A, [U-100% 13C; U-100% 15N], 0.8 mM; potassium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.2%

sample_4: forC/ A, [U-100% 13C; U-100% 15N], 0.8 mM; potassium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.2 % v/v; C12E5 8.6 % w/v; hexanol 2 % v/v

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D CCONH-TOCSYsample_2isotropicsample_conditions_1
3D CBCANHsample_2isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D HACAHB-COSYsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
2D 13C-{13CO}-1H-13C HSQCsample_2isotropicsample_conditions_1
2D 13C-{15N}-1H-13C HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1
2D 1H-15N HSQC-IPAPsample_4isotropicsample_conditions_1
3D HN(CO)CA_Jcahasample_4isotropicsample_conditions_1
3D HN(CO)CA_Jcacbsample_4isotropicsample_conditions_1
{1H}-15N-NOEsample_1isotropicsample_conditions_1
15N-T1sample_1isotropicsample_conditions_1
15N-T2sample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1

Software:

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

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

PDB
DBJ BAC16798
GB EAL63715
REF XP_637272
SP Q54KF1

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