BMRB Entry 34111

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34111
MolProbity Validation Chart

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Title:
Structure of the N-terminal domain of the Escherichia Coli ProQ RNA binding protein
Deposition date:
2017-03-01
Original release date:
2017-05-04
Authors:
Gonzales, G.; Hardwick, S.; Maslen, S.; Skehel, M.; Holmqvist, E.; Vogel, J.; Bateman, A.; Luisi, B.; Broadhurst, R.
Citation:

Citation: Gonzalez, G.; Hardwick, S.; Maslen, S.; Skehel, J.; Holmqvist, E.; Vogel, J.; Bateman, A.; Luisi, B.; Broadhurst, R.. "Structure of the Escherichia coli ProQ RNA-binding protein."  RNA 23, 696-711 (2017).
PubMed: 28193673

Assembly members:

Assembly members:
entity_1, polymer, 53 residues, 5601.499 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 83333   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: ProQ-pET-DUET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: VSDISALTVGQALKVKAGQN AMDATVLEITKDGVRVQLNS GMSLIVRAEHLVF

Data sets:
Data typeCount
13C chemical shifts156
15N chemical shifts54
1H chemical shifts349

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 53 residues - 5601.499 Da.

1   VALSERASPILESERALALEUTHRVALGLY
2   GLNALALEULYSVALLYSALAGLYGLNASN
3   ALAMETASPALATHRVALLEUGLUILETHR
4   LYSASPGLYVALARGVALGLNLEUASNSER
5   GLYMETSERLEUILEVALARGALAGLUHIS
6   LEUVALPHE

Samples:

sample_1: entity_1 mM; 3,3,3-trimethylsilylpropionate 0.0025 ± 0.0005 %; TCEP 1 ± 0.1 mM; sodium chloride 100 ± 5 mM; sodium phosphate 20 ± 1 mM

sample_2: entity_1 mM; 3,3,3-trimethylsilylpropionate 0.0025 ± 0.0005 %; TCEP 1 ± 0.1 mM; sodium chloride 20 ± 1 mM; sodium phosphate 100 ± 5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

ARIA v2.3, Linge, O'Donoghue and Nilges - structure calculation

Analysis v2.4, CCPN - data analysis

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

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