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 34163

Title: Structure of DNA-binding HU protein from micoplasma Spiroplasma melliferum

Authors: Altukhov, D.; Talyzina, A.; Agapova, Y.; Vlaskina, A.; Korzhenevskiy, D.; Bocharov, E.; Rakitina, T.; Timofeev, V.

Citation: Altukhov, D.; Talyzina, A.; Agapova, Y.; Vlaskina, A.; Korzhenevskiy, D.; Bocharov, E.; Rakitina, T.; Timofeev, V.. "Structure of DNA-binding HU protein from micoplasma Spiroplasma melliferum"  . ., .-..

Assembly members:
DNA-binding protein, polymer, 95 residues, 10291.794 Da.

Natural source:   Common Name: Spiroplasma melliferum KC3   Taxonomy ID: 570509   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Spiroplasma Melliferum

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

Entity Sequences (FASTA):
DNA-binding protein: GHMSKKELAAQIAEKFTDVL SKTHAEEITNFVFDHIKKAL VAGKEVSIAGFGKFAVTERA ARDGRNPSTGETIKIPASKS AKFKAGKQLKTDLNN

Data sets:
Data typeCount
13C chemical shifts119
15N chemical shifts78
1H chemical shifts123

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_1, chain 11
2entity_1, chain 21

Entities:

Entity 1, entity_1, chain 1 95 residues - 10291.794 Da.

1   GLYHISMETSERLYSLYSGLULEUALAALA
2   GLNILEALAGLULYSPHETHRASPVALLEU
3   SERLYSTHRHISALAGLUGLUILETHRASN
4   PHEVALPHEASPHISILELYSLYSALALEU
5   VALALAGLYLYSGLUVALSERILEALAGLY
6   PHEGLYLYSPHEALAVALTHRGLUARGALA
7   ALAARGASPGLYARGASNPROSERTHRGLY
8   GLUTHRILELYSILEPROALASERLYSSER
9   ALALYSPHELYSALAGLYLYSGLNLEULYS
10   THRASPLEUASNASN

Samples:

sample_1: entity_1, na, mM; D2O, [U-2H], 5%

sample_conditions_1: ionic strength: 0.375 M; pH: 6.7; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

GROMACS, Herman Berendsen's group, department of Biophysical Chemistry of Groningen University - refinement

TALOS++, Cornilescu, Delaglio and Bax - chemical shift assignment

NMR spectrometers:

  • Agilent Uniform NMR System 700 MHz

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