BMRB Entry 25296

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25296
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Hha-H-NS46 charge zipper complex
Deposition date:
2014-10-24
Original release date:
2015-07-27
Authors:
Cordeiro, Tiago; Garcia, Jesus; Bernado, Pau; Millet, Oscar; Pons, Miquel
Citation:

Citation: Cordeiro, Tiago; Garcia, Jesus; Bernado, Pau; Millet, Oscar; Pons, Miquel. "A Three-protein Charge Zipper Stabilizes a Complex Modulating Bacterial Gene Silencing."  J. Biol. Chem. 290, 21200-21212 (2015).
PubMed: 26085102

Assembly members:

Assembly members:
entity_1, polymer, 69 residues, 8068.402 Da.
entity_2, polymer, 46 residues, 5177.926 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: EKLTKTDYLMRLRRCQTIDT LERVIEKNKYELSDNELAVF YSAADHRLAELTMNKLYDKI PSSVWKFIR
entity_2: SEALKILNNIRTLRAQAREC TLETLEEMLEKLEVVVNERR EEESAA

Data sets:
Data typeCount
15N chemical shifts115
1H chemical shifts120

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_2_12
3entity_2_22

Entities:

Entity 1, entity_1 69 residues - 8068.402 Da.

1   GLULYSLEUTHRLYSTHRASPTYRLEUMET
2   ARGLEUARGARGCYSGLNTHRILEASPTHR
3   LEUGLUARGVALILEGLULYSASNLYSTYR
4   GLULEUSERASPASNGLULEUALAVALPHE
5   TYRSERALAALAASPHISARGLEUALAGLU
6   LEUTHRMETASNLYSLEUTYRASPLYSILE
7   PROSERSERVALTRPLYSPHEILEARG

Entity 2, entity_2_1 46 residues - 5177.926 Da.

1   SERGLUALALEULYSILELEUASNASNILE
2   ARGTHRLEUARGALAGLNALAARGGLUCYS
3   THRLEUGLUTHRLEUGLUGLUMETLEUGLU
4   LYSLEUGLUVALVALVALASNGLUARGARG
5   GLUGLUGLUSERALAALA

Samples:

sample_3: entity_1, [U-100% 15N], 0.9 mM; sodium chloride 150 mM; sodium azide 0.01 w/v; sodium phosphate 20 mM; H2O 90%; D2O 10%

sample_4: entity_2, [U-100% 15N], 0.9 mM; sodium chloride 150 mM; sodium azide 0.01 w/v; sodium phosphate 20 mM; H2O 90%; D2O 10%

sample_1: entity_10.015 – 0.030 mM; entity_2, [U-100% 15N], 0.10 mM; HEPES 20 mM; sodium chloride 150 mM; sodium azide 0.01 w/v; H2O 90%; D2O 10%

sample_2: entity_10.015 – 0.030 mM; entity_2, [U-100% 15N], 0.10 mM; HEPES 20 mM; sodium chloride 150 mM; sodium azide 0.01 w/v; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.16 M; pH: 7.0; pressure: 1 atm; temperature: 295 K

sample_conditions_2: ionic strength: 0.20 M; pH: 7.0; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_2
3D 1H-15N NOESYsample_3isotropicsample_conditions_2
3D 1H-15N TOCSYsample_3isotropicsample_conditions_2
2D 1H-15N HSQCsample_4isotropicsample_conditions_2
3D 1H-15N NOESYsample_4isotropicsample_conditions_2
3D 1H-15N TOCSYsample_4isotropicsample_conditions_2

Software:

NMRPipe, Delaglio, Zhengrong and Bax - processing

NMRView, Johnson, One Moon Scientific - peak picking

CARA, Keller and Wuthrich - chemical shift assignment

CNS v2.0, Brunger, Adams, Clore, Gros, Nilges and Read - Calculation Engine

Haddock v2.1, Alexandre Bonvin - Data-driven docking using cns as structure calculation engine

TOPSPIN, Bruker Biospin - nmr spectra acquisition

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance III 600 MHz

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