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Biological Magnetic Resonance Data Bank


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BMRB Entry 15314

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15314
MolProbity Validation Chart

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Title: Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from the phytopathogen Xylella fastidiosa.

Deposition date: 2007-06-18 Original release date: 2009-10-14

Authors: Rosselli, Luciana; Sforca, Mauricio; Souza, Anete; Zeri, Ana

Citation: Rosselli, Luciana; Sforca, Mauricio; Souza, Anete; Zeri, Ana. "Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from the phytopathogen Xylella fastidiosa."  Not known ., .-..

Assembly members:
protein_HNS79c, polymer, 79 residues, 8857.435 Da.

Natural source:   Common Name: Xylella fastidiosa   Taxonomy ID: 2371   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Xylella fastidiosa

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

Entity Sequences (FASTA):
protein_HNS79c: FNVKQKSEITALVKEVTPPR KAPSKAKREAPIKYWLPHSG ATWSGRGKIPKPFEAWIGTA AYTAWKAKHPDEKFPAFPG

Data sets:
Data typeCount
13C chemical shifts303
15N chemical shifts74
1H chemical shifts516

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1HNS79c1

Entities:

Entity 1, HNS79c 79 residues - 8857.435 Da.

1   PHEASNVALLYSGLNLYSSERGLUILETHR
2   ALALEUVALLYSGLUVALTHRPROPROARG
3   LYSALAPROSERLYSALALYSARGGLUALA
4   PROILELYSTYRTRPLEUPROHISSERGLY
5   ALATHRTRPSERGLYARGGLYLYSILEPRO
6   LYSPROPHEGLUALATRPILEGLYTHRALA
7   ALATYRTHRALATRPLYSALALYSHISPRO
8   ASPGLULYSPHEPROALAPHEPROGLY

Samples:

sample_1: protein_HNS79c, [U-99% 13C; U-99% 15N], 0.5 mM; sodium phosphate 50 mM; NaCl 200 mM; sodium azide 1%; H2O 95%; D2O 5%

sample_2: protein_HNS79c, [U-99% 13C; U-99% 15N], 0.5 mM; sodium phosphate 50 mM; NaCl 200 mM; sodium azide 1%; D2O 100%

sample_3: protein_HNS79c, [U-99% 15N], 0.5 mM; sodium phosphate 50 mM; NaCl 200 mM; sodium azide 1%; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.25 M; pH: 6.8; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D CCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
Heteronuclear NOEsample_3isotropicsample_conditions_1
Heteronuclear NOEsample_3isotropicsample_conditions_1
T1 Relaxationsample_3isotropicsample_conditions_1
T1 Relaxationsample_3isotropicsample_conditions_1
T2 Relaxationsample_3isotropicsample_conditions_1
T2 Relaxationsample_3isotropicsample_conditions_1

Software:

NMRPipe v5.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v5.0, Johnson, One Moon Scientific - chemical shift assignment

DYANA, Guntert, Braun and Wuthrich - geometry optimization, structure solution

DISCOVER, Accelrys Software Inc. - energy minimization, refinement

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB AAF83559 AAO29736 ACA12952 ACB93409 ADN62770
REF WP_004090416 WP_010893272 WP_020852461 WP_057682395

Download simulated HSQC data in one of the following formats:
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