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 15527

Title: 1H, 13C, and 31P Chemical Shift Assignments for 14-mer Base Pair Non-self Complementary DNA Duplex ( Mbp1_14) which Contains the Consensus Binding Site of the Yeast Transcription Factor Mbp-1

Authors: Chernatynskaya, Anna; Lane, Andrew

Citation: Deleeuw, Lynn; Chernatynskaya, Anna; Lane, Andrew. "Structural analysis of the DNA target site and its interaction with Mbp1"  Org. Biomol. Chem. ., .-..

Assembly members:
DNA_Strand1, polymer, 14 residues, Formula weight is not available
DNA_Strand2, polymer, 14 residues, Formula weight is not available

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: obtained from a vendor

Entity Sequences (FASTA):
DNA_Strand1: CTTACGCGTCATTG
DNA_Strand2: CAATGACGCGTAAG

Data sets:
Data typeCount
13C chemical shifts116
1H chemical shifts227
31P chemical shifts25

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1DNA Starnd11
2DNA Strand22

Entities:

Entity 1, DNA Starnd1 14 residues - Formula weight is not available

1   DCDTDTDADCDGDCDGDTDC
2   DADTDTDG

Entity 2, DNA Strand2 14 residues - Formula weight is not available

1   DCDADADTDGDADCDGDCDG
2   DTDADADG

Samples:

sample_1: sodium phosphate 10 mM; sodium chloride 100 mM; Mbp1_14 1.2 mM; H2O 100%

sample_2: sodium phosphate 10 mM; sodium chloride 100 mM; Mbp1_14 1.2 mM; H2O 90%; D2O 10%

sample_3: sodium phosphate 10 mM; sodium chloride 100 mM; Mbp1_14, [U-13C], 0.4 mM; Mbp1_14 0.4 mM; H2O 100%

sample_4: sodium phosphate 10 mM; sodium chloride 100 mM; Mbp1_14, [U-13C], 0.4 mM; Mbp1_14 0.4 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7; temperature: 303 K

sample_conditions_2: pH: 7; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
WGNOESYsample_2isotropicsample_conditions_2
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-31P HSQCsample_1isotropicsample_conditions_1
2D 1H-13C NOESY-HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_4isotropicsample_conditions_1

Software:

VNMR v6.1, Varian - processing

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

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