BMRB Entry 16948

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16948

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Title:
Resonance assignments of GTPase effector domain of Dynamin in the aprotic solvent deuterated Dimethyl Sulfoxide
Deposition date:
2010-05-24
Original release date:
2011-05-24
Authors:
Hosur, Ramakrishna; Chakraborty, Swagata
Citation:

Citation: Chakraborty, Swagata; Hosur, Ramakrishna. "Resonance assignments of GTPase effector domain of dynamin in the aprotic solvent deuterated dimethyl sulfoxide."  Biomol. NMR Assignments 5, 59-61 (2011).
PubMed: 20936383

Assembly members:

Assembly members:
GTPase_Effector_Domain_(GED), polymer, 138 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX4T1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GTPase_Effector_Domain_(GED): GSASFLRAGVYPERVGDKEK ASETEENGSDSFMHSMDPQL ERQVETIRNLVDSYMAIVNK TVRDLMPKTIMHLMINNTKE FIFSELLANLYSCGDQNTLM EESAEQAQRRDEMLRMYHAL KEALSIIGNINTTTVSTP

Data sets:
Data typeCount
13C chemical shifts366
15N chemical shifts124
1H chemical shifts667

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Dynamin1

Entities:

Entity 1, Dynamin 138 residues - Formula weight is not available

1   GLYSERALASERPHELEUARGALAGLYVAL
2   TYRPROGLUARGVALGLYASPLYSGLULYS
3   ALASERGLUTHRGLUGLUASNGLYSERASP
4   SERPHEMETHISSERMETASPPROGLNLEU
5   GLUARGGLNVALGLUTHRILEARGASNLEU
6   VALASPSERTYRMETALAILEVALASNLYS
7   THRVALARGASPLEUMETPROLYSTHRILE
8   METHISLEUMETILEASNASNTHRLYSGLU
9   PHEILEPHESERGLULEULEUALAASNLEU
10   TYRSERCYSGLYASPGLNASNTHRLEUMET
11   GLUGLUSERALAGLUGLNALAGLNARGARG
12   ASPGLUMETLEUARGMETTYRHISALALEU
13   LYSGLUALALEUSERILEILEGLYASNILE
14   ASNTHRTHRTHRVALSERTHRPRO

Samples:

sample_1: GTPase Effector Domain (GED), [U-100% 13C; U-100% 15N], 1 – 1.5 mM; DMSO 100%; Sodium chloride 150 mM; Acetate buffer 20 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNNsample_1isotropicsample_conditions_1

Software:

CARA v1.8.4.2, Rochus Keller - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 15867 15868
PDB
DBJ BAD90284 BAE25726 BAG53342 BAG58137 BAG59018
EMBL CAA38397
GB AAA02803 AAA37318 AAA37319 AAA37323 AAA37324
PIR B40671
PRF 1614348A
REF NP_001005336 NP_001070288 NP_001124521 NP_001275666 NP_001275667
SP P21575 P39053 Q05193 Q08DF4
TPG DAA24145
AlphaFold P21575 P39053 Q05193 Q08DF4

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