BMRB Entry 7225

Title:
Solution NMR structure of the UPF0291 protein ynzC from Bacillus subtilis. Northeast Structural Genomics target SR384. (CASP Target)
Deposition date:
2006-07-14
Original release date:
2008-07-16
Authors:
Aramini, J.; Swapna, G.; Ho, C.; Shetty, K.; Cunningham, K.; Ma, L.-C.; Xiao, R.; Liu, J.; Baran, M.; Acton, T.; Rost, B.; Montelione, G.
Citation:

Citation: Aramini, J.; Sharma, S.; Huang, Y.; Swapna, G.; Ho, C.; Shetty, K.; Cunningham, K.; Ma, L.-C.; Zhao, L.; Owens, L.; Jiang, M.; Xiao, R.; Liu, J.; Baran, M.; Acton, T.; Rost, B.; Montelione, G.. "Solution NMR structure of the SOS response protein YnzC from Bacillus subtilis"  Proteins 72, 526-530 (2008).
PubMed: 18431750

Assembly members:

Assembly members:
UPF0291 protein ynzC, polymer, 85 residues, Formula weight is not available

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts338
15N chemical shifts75
1H chemical shifts489

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UPF0291 protein ynzC1

Entities:

Entity 1, UPF0291 protein ynzC 85 residues - Formula weight is not available

1   METILESERASNALALYSILEALAARGILE
2   ASNGLULEUALAALALYSALALYSALAGLY
3   VALILETHRGLUGLUGLULYSALAGLUGLN
4   GLNLYSLEUARGGLNGLUTYRLEULYSGLY
5   PHEARGSERSERMETLYSASNTHRLEULYS
6   SERVALLYSILEILEASPPROGLUGLYASN
7   ASPVALTHRPROGLULYSLEULYSARGGLU
8   GLNARGASNASNLYSLEUHISLEUGLUHIS
9   HISHISHISHISHIS

Samples:

sample_1: UPF0291 protein ynzC, [U-13C; U-15N], 1.12 mM; MES 20 mM; NaCl 100 mM; CaCl2 5 mM; DTT 10 mM; NaN3 0.02%; D2O 5%; H2O 95%

sample_2: UPF0291 protein ynzC, [U-5% 13C; U-15N], 1.12 mM; MES 20 mM; NaCl 100 mM; CaCl2 5 mM; DTT 10 mM; NaN3 0.02%; D2O 5%; H2O 95%

sample_cond_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYnot availablenot availablenot available
3D 13C-separated NOESYnot availablenot availablenot available
HNHAnot availablenot availablenot available
3D GFT-CBCACAcoNHNnot availablenot availablenot available
GFT-HNNCACBCAnot availablenot availablenot available
GFT-HABCABcoNHNnot availablenot availablenot available
3D HCCH-TOCSYnot availablenot availablenot available
CCcoNH TOCSYnot availablenot availablenot available
HCCH-COSYnot availablenot availablenot available
high resolution 2D CH-HQSC (for stereospecific assignment of Val/Leu methyls)not availablenot availablenot available
3D HNCOnot availablenot availablenot available
HNcaCOnot availablenot availablenot available
2D 15N1H-heteronuclear NOEnot availablenot availablenot available

Software:

VNMR v6.1C - collection

xwinnmr v3.5pl6 - collection

AutoAssign v2.2.1 - data analysis

SPARKY v3.110 - data analysis

AutoStruct v2.1.1 - refinement

X-PLOR NIH v2.11.2 - refinement

AGNUS v2.0 - data analysis

PDBStat v4.01 - data analysis

PSVS v1.2 - data analysis

NMR spectrometers:

  • Bruker AVANCE 600 MHz

Related Database Links:

BMRB 15476
PDB
DBJ BAI85472 BAM52440 BAM58016 GAK81555
EMBL CAB13672 CCU58402 CEI56979 CEJ77403
GB ADV92690 AEP90959 AFI28488 AFQ57722 AGE63629
REF NP_389671 WP_003231595 WP_014664125 WP_019714523 WP_024573193
SP O31818
AlphaFold O31818

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