BMRB Entry 28112

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28112
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Title:
1H, 13C, and 15N chemical shift assignments of the Gp4 from the Pseudomonas phage LUZ24
Deposition date:
2020-04-10
Original release date:
2021-05-07
Authors:
Volkov, Alexander; Bdira, Fredj; Dame, Remus
Citation:

Citation: Bdira, Fredj Ben; Erkelens, Amanda; Qin, Liang; Volkov, Alexander; Lippa, Andrew; Bowring, Nicholas; Boyle, Aimee; Ubbink, Marcellus; Dove, Simon; Dame, Remus. "Novel anti-repression mechanism of H-NS proteins by a phage protein"  Nucleic Acids Res. 49, 10770-10784 (2021).
PubMed: 34520554

Assembly members:

Assembly members:
Gp4, polymer, 46 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Pseudomonas phage LUZ24   Taxonomy ID: 484895   Superkingdom: Viruses   Kingdom: not available   Genus/species: Bruynoghevirus Pseudomonas phage LUZ24

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET30b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Gp4: MKSPYEAAHERALMVNRLQK LTRMLRVHPDPKWKQEQQEL IKRLKK

Data sets:
Data typeCount
13C chemical shifts229
15N chemical shifts47
1H chemical shifts366

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Gp4 from the Pseudomonas phage LUZ241

Entities:

Entity 1, Gp4 from the Pseudomonas phage LUZ24 46 residues - Formula weight is not available

1   METLYSSERPROTYRGLUALAALAHISGLU
2   ARGALALEUMETVALASNARGLEUGLNLYS
3   LEUTHRARGMETLEUARGVALHISPROASP
4   PROLYSTRPLYSGLNGLUGLNGLNGLULEU
5   ILELYSARGLEULYSLYS

Samples:

sample_1: Gp4, [U-13C; U-15N], 1 mM; Bis-TRIS 20 mM; potassium chloride 150 mM; EDTA 1 mM; D2O, [U-100% 2H], 6%

sample_conditions_1: ionic strength: 170 mM; pH: 6; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D H(C)CH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CCPN, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • 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