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 16378

Title: Chemical shift assignment of GtR34C from Geobacillus thermodenitrificans. North East Structural Genomics Consortium Target GtR34C

Deposition date: 2009-06-29 Original release date: 2009-07-07

Authors: Lee, Hsiau-Wei; Wang, Huang; Ciccosanti, Colleen; Jiang, Mei; Nair, R; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Swapna, GVT; Evertt, John; Montelione, Gaetano; Prestegard, James

Citation: Lee, Hsiau-Wei; Montelione, Gaetano; Prestegard, James. "Solution Structure of GtR34C"  Not known ., .-..

Assembly members:
GtR34C, polymer, 174 residues, 19278.225 Da.

Natural source:   Common Name: Geobacillus thermodenitrificans   Taxonomy ID: 33940   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Geobacillus thermodenitrificans

Experimental source:   Production method: recombinant technology   Host organism: Geobacillus thermodenitrificans

Entity Sequences (FASTA):
GtR34C: MNEAKGVYVMSVLPNMPAAG RLEAGDRIAAIDGQPINTSE QIVSYVREKQAGDRVRVTFI RDRKQHEAELVLKPFPHHPN QIGLGVTMNEAKGVYVMSVL PNMPAAGRLEAGDRIAAIDG QPINTSEQIVSYVREKQAGD RVRVTFIRDRKQHEAELVLK PFPHHPNQIGLGVT

Data sets:
Data typeCount
13C chemical shifts324
15N chemical shifts76
1H chemical shifts523
residual dipolar couplings125

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GtR34C1

Entities:

Entity 1, GtR34C 174 residues - 19278.225 Da.

LEHHHHHH are at the C-terminal as part of Hig-Tag. It is not included in the coordinate file.

1   METASNGLUALALYSGLYVALTYRVALMET
2   SERVALLEUPROASNMETPROALAALAGLY
3   ARGLEUGLUALAGLYASPARGILEALAALA
4   ILEASPGLYGLNPROILEASNTHRSERGLU
5   GLNILEVALSERTYRVALARGGLULYSGLN
6   ALAGLYASPARGVALARGVALTHRPHEILE
7   ARGASPARGLYSGLNHISGLUALAGLULEU
8   VALLEULYSPROPHEPROHISHISPROASN
9   GLNILEGLYLEUGLYVALTHRMETASNGLU
10   ALALYSGLYVALTYRVALMETSERVALLEU
11   PROASNMETPROALAALAGLYARGLEUGLU
12   ALAGLYASPARGILEALAALAILEASPGLY
13   GLNPROILEASNTHRSERGLUGLNILEVAL
14   SERTYRVALARGGLULYSGLNALAGLYASP
15   ARGVALARGVALTHRPHEILEARGASPARG
16   LYSGLNHISGLUALAGLULEUVALLEULYS
17   PROPHEPROHISHISPROASNGLNILEGLY
18   LEUGLYVALTHR

Samples:

sample_1: GtR34C, [U-100% 13C; U-100% 15N], 1.14 mM; sodium azide 2%; DTT 10 mM; CaCl 5 mM; sodium chloride 200 mM; MES 20 mM; H2O 95%; D2O 5%

PEG: GtR34C, [U-100% 13C; U-100% 15N], 1.14 mM; sodium azide 2%; DTT 10 mM; CaCl 5 mM; sodium chloride 200 mM; MES 20 mM; C12E5 PEG/Hexanol 4.2%; H2O 95%; D2O 5%

GEL: GtR34C, [U-100% 13C; U-100% 15N], 1.14 mM; sodium azide 2%; DTT 10 mM; CaCl 5 mM; sodium chloride 200 mM; MES 20 mM; Negatively Charged Compressed Polyacrylamide Gel 7%; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: ambient atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 15N HSQCTROSYPEGisotropicsample_conditions_1
2D 15N HSQCTROSYGELisotropicsample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR NIH v2.18, Schwieters, Kuszewski, Tjandra and Clore - refinement

SPARKY, Goddard - chemical shift assignment

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

PSVS, Bhattacharya and Montelione - data analysis

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

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB

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