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 34110

Title: Structure of the N-terminal domain of the Escherichia Coli ProQ RNA binding protein   PubMed: 28193673

Authors: Gonzales, G.; Hardwick, S.; Maslen, S.; Skehel, M.; Holmqvist, E.; Vogel, J.; Bateman, A.; Luisi, B.; Broadhurst, R.

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).

Assembly members:
entity_1, polymer, 133 residues, 15107.911 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 585035   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSQDPMENQPK LNSSKEVIAFLAERFPHCFS AEGEARPLKIGIFQDLVDRV AGEMNLSKTQLRSALRLYTS SWRYLYGVKPGATRVDLDGN PCGELDEQHVEHARKQLEEA KARVQAQRAEQQA

Data sets:
Data typeCount
13C chemical shifts493
15N chemical shifts126
1H chemical shifts722

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 133 residues - 15107.911 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERGLNASPPROMETGLUASNGLNPROLYS
3   LEUASNSERSERLYSGLUVALILEALAPHE
4   LEUALAGLUARGPHEPROHISCYSPHESER
5   ALAGLUGLYGLUALAARGPROLEULYSILE
6   GLYILEPHEGLNASPLEUVALASPARGVAL
7   ALAGLYGLUMETASNLEUSERLYSTHRGLN
8   LEUARGSERALALEUARGLEUTYRTHRSER
9   SERTRPARGTYRLEUTYRGLYVALLYSPRO
10   GLYALATHRARGVALASPLEUASPGLYASN
11   PROCYSGLYGLULEUASPGLUGLNHISVAL
12   GLUHISALAARGLYSGLNLEUGLUGLUALA
13   LYSALAARGVALGLNALAGLNARGALAGLU
14   GLNGLNALA

Samples:

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

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

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_2
3D HN(CO)CAsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_2
3D CBCA(CO)NHsample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2
3D 1H-13C NOESYsample_2isotropicsample_conditions_2
2D 1H-13C HSQCsample_2isotropicsample_conditions_2

Software:

Analysis v2.4, CCPN - data analysis

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

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker Avance 600 MHz

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