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Biological Magnetic Resonance Data Bank


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BMRB Entry 16335

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16335
MolProbity Validation Chart

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Title: Solution structure of protein YlbL (BSU15050) from Bacillus subtilis, Northeast Structural Genomics Consortium target sr713a

Deposition date: 2009-06-05 Original release date: 2012-08-03

Authors: Liu, Yizhou; Belote, Rachel; Ciccosanti, Colleen; Hamilton, Keith; Nair, R.; Rost, B.; Acton, T.; Xiao, R.; Swapna, G.; Everett, J.; Montelione, G.; Prestegard, James

Citation: Liu, Yizhou; Belote, Rachel; Ciccosanti, Colleen; Hamilton, Keith; Nair, R.; Rost, B.; Acton, T.; Xiao, R.; Swapna, G.; Everett, J.; Montelione, G.; Prestegard, James. "Resonance assignment protein YLBL(BSU15050), Northeast Structural Genomics Consortium Target sr713a"  Not known ., .-..

Assembly members:
BSU15050, polymer, 91 residues, 20921.646 Da.

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

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

Entity Sequences (FASTA):
BSU15050: NGIYASSVVENMPAKGKIEV GDKIISADGKNYQSAEKLID YISSKKAGDKVTLKIEREEK EKRVTLTLKQFPDEPDRAGI GVSLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts307
15N chemical shifts73
1H chemical shifts491

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BSU150501

Entities:

Entity 1, BSU15050 91 residues - 20921.646 Da.

1   ASNGLYILETYRALASERSERVALVALGLU
2   ASNMETPROALALYSGLYLYSILEGLUVAL
3   GLYASPLYSILEILESERALAASPGLYLYS
4   ASNTYRGLNSERALAGLULYSLEUILEASP
5   TYRILESERSERLYSLYSALAGLYASPLYS
6   VALTHRLEULYSILEGLUARGGLUGLULYS
7   GLULYSARGVALTHRLEUTHRLEULYSGLN
8   PHEPROASPGLUPROASPARGALAGLYILE
9   GLYVALSERLEUGLUHISHISHISHISHIS
10   HIS

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 0.5 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 100 mM; sodium azide 3 mM; H2O 95%; D2O 10%

sample_2: entity, [U-99% 13C; U-99% 15N], 0.5 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 5 mM; sodium azide 3 mM; D2O 100%

sample_3: entity, [U-99% 15N], 0.5 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 100 mM; sodium azide 3 mM; H2O 95%; D2O 10%

sample_conditions_1: ionic strength: 0.3 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
TROSY-HSQCsample_3isotropicsample_conditions_1
TROSY-HSQCsample_3anisotropicsample_conditions_1

Software:

VNMR, Varian - collection

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAI85130 BAM52152 BAM57728 GAK80480
EMBL CAB11358 CAB13378 CCU58075 CEI56686 CEJ77092
GB ADM37598 ADV96527 AEP86489 AEP90657 AFQ57441
REF NP_389388 WP_003221384 WP_003245451 WP_009967176 WP_010328046
SP O34470

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