BMRB Entry 16384

Title:
Solution NMR Structure of protein yutD from B.subtilis, Northeast Structural Genomics Consortium Target Target SR232
Deposition date:
2009-06-30
Original release date:
2009-07-07
Authors:
Liu, G.; Hamilton, H.; Xiao, R.; Ciccosanti, C.; Ho, K.; Everett, J.; Nair, R.; Acton, T.; Rost, B.; Montelione, G.
Citation:

Citation: Liu, G.; Hamilton, H.; Xiao, R.; Ciccosanti, C.; Ho, K.; Everett, J.; Nair, R.; Acton, T.; Rost, B.; Montelione, G.. "Solution NMR Structure of protein yutD from B.subtilis, Northeast Structural Genomics Consortium Target Target SR232"  To be published ., .-..

Assembly members:

Assembly members:
SR232, polymer, 110 residues, 13241.087 Da.

Natural source:

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: BL21

Data sets:
Data typeCount
13C chemical shifts382
15N chemical shifts72
1H chemical shifts623

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SR2321

Entities:

Entity 1, SR232 110 residues - 13241.087 Da.

1   METILEGLYMETSERGLULYSARGGLYGLU
2   ILEMETILELEUILEGLNASNALAGLUPHE
3   GLULEUVALHISASNPHELYSASPGLYPHE
4   ASNGLUGLUALAPHELYSALAARGTYRSER
5   ASPILELEUASNLYSTYRASPTYRILEVAL
6   GLYASPTRPGLYTYRGLYGLNLEUARGLEU
7   LYSGLYPHEPHEASPASPGLNASNGLNLYS
8   ALATHRPHEGLUTHRLYSILESERTHRLEU
9   ASPGLUTYRILETYRGLUTYRCYSASNPHE
10   GLYCYSALATYRPHEVALLEULYSARGILE
11   ARGLYSLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: SR232, [U-100% 13C; U-100% 15N], 1.1 mM; DTT 10 mM; Arginine 50 mM; Bis-Tris pH 6.5 50 mM; DSS 50 uM; NaN3 0.02%; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-13C arom NOESYsample_1isotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

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

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis

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

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAI86771 BAM55300 BAM59313 GAK81980
EMBL CAB15221 CCU60272 CEI58480 CEJ78885 CJS52863
GB ADM39188 ADV94035 AEP88101 AEP92247 AFI29777
REF NP_391111 WP_003222892 WP_003228682 WP_010329969 WP_017696728
SP O32127
AlphaFold O32127

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