BMRB Entry 5920

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5920
MolProbity Validation Chart

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Title:
1H, 13C and 15N backbone and side-chain chemical shift assignments of PrrA effector domain from R. sphaeroides
Deposition date:
2003-08-26
Original release date:
2003-12-19
Authors:
Laguri, Cedric; Phillips-jones, Mary; Williamson, Mike
Citation:

Citation: Laguri, Cedric; Phillips-jones, Mary; Williamson, Mike. "Solution structure and DNA binding of the effector domain from the global regulator PrrA (RegA) from R. sphaeroides: insights into binding specificity "  Nucleic Acids Res. 31, 6778-6787 (2003).
PubMed: 14627811

Assembly members:

Assembly members:
PrrA, polymer, 81 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Rhodobacter sphaeroides   Taxonomy ID: 1063   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Rhodobacter sphaeroides

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PET14a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PrrA: MGSSHHHHHHSSGLVPRGSH MLAKGESLPPPPENPMSADR VRWEHIQRIYEMCDRNVSET ARRLNMHRRTLQRILAKRSP R

Data sets:
Data typeCount
1H chemical shifts548
13C chemical shifts344
15N chemical shifts89

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1PrrAC1

Entities:

Entity 1, PrrAC 81 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METLEUALALYSGLYGLUSERLEUPROPRO
4   PROPROGLUASNPROMETSERALAASPARG
5   VALARGTRPGLUHISILEGLNARGILETYR
6   GLUMETCYSASPARGASNVALSERGLUTHR
7   ALAARGARGLEUASNMETHISARGARGTHR
8   LEUGLNARGILELEUALALYSARGSERPRO
9   ARG

Samples:

sample_1: PrrA, [U-95% 13C; U-95% 15N], 1.0 mM; ammonium sulfate 200 mM; NaCl 50 mM; sodium phosphate 50 mM; DTT 10 mM

Standard_condition: pH: 6.0; temperature: 275 K; ionic strength: 0.6 M

Experiments:

NameSampleSample stateSample conditions

Software:

felix v2000 -

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker DRX 600 MHz

Related Database Links:

PDB
EMBL CAA54059
GB AAA16649 ABA77661 ABN75289 ABP71845 ACM02772
REF WP_002722225 WP_011909904 WP_015921751 YP_001042061 YP_001169150
SP Q53228
AlphaFold Q53228

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