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 15476

Title: Solution NMR structure of the folded N-terminal fragment of UPF0291 protein ynzC from Bacillus subtilis. Northeast Structural Genomics target SR384-1-46.   PubMed: 18431750

Authors: Aramini, James; Sharma, Seema; Huang, Yuanpeng; Zhao, Li; Owens, Leah; Stokes, Kate; Jiang, Mei; Xiao, Rong; Baran, Micheal; Swapna, Gurla; Acton, Thomas; Montelione, Gaetano

Citation: Aramini, James; Sharma, Seema; Huang, Yuanpeng; Swapna, Gurla; Ho, Chi Kent; Shetty, Karishma; Cunningham, Kellie; Ma, Li-Chung; Zhao, Li; Owens, Leah; Jiang, Mei; Xiao, Rong; Liu, Jinfeng; Baran, Micheal; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano. "Solution NMR structure of the SOS response protein YnzC from Bacillus subtilis"  Proteins 72, 526-530 (2008).

Assembly members:
SR384-1-46, polymer, 54 residues, 6290.301 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):

Data sets:
Data typeCount
13C chemical shifts221
15N chemical shifts52
1H chemical shifts356

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Entity Assembly IDEntity NameEntity ID


Entity 1, SR384-1-46 54 residues - 6290.301 Da.

C-terminal LEHHHHHH purification tag starting at residue 47.



sample_1: SR384-1-46, [U-100% 13C; U-100% 15N], 1.36 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; calcium chloride 5 mM; sodium azide 0.02%

sample_2: SR384-1-46, [U-5% 13C; U-100% 15N], 1.1 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; calcium chloride 5 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K


NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC (aliph)sample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D simultaneous CN-NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
2D 1H-13C HSQC stereospecific Leu/Val methylsample_2isotropicsample_conditions_1
2D 1H-13C HSQC (arom)sample_1isotropicsample_conditions_1


TOPSPIN v1.3, Bruker Biospin - collection

AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - data analysis, RPF calculation

PSVS v1.3, Bhattacharya and Montelione - structure validation

PDBStat v5.0, Tejero and Montelione - PDB analysis

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Th - structure validation

MolProbity, Richardson - structure validation

SPARKY v3.110, Goddard - data analysis, peak picking

VNMR v6.1C, Varian - collection

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

DBJ BAI85472 BAM52440 BAM58016 GAK81555
EMBL CAB13672 CCU58402 CEI56979 CEJ77403 CJS75223
GB ADV92690 AEP86787 AEP90959 AFI28488 AFQ57722
REF NP_389671 WP_003231595 WP_010330660 WP_014113934 WP_014664125
SP O31818