BMRB Entry 50711

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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/BMR50711
MolProbity Validation Chart

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Title:
1H, 13C, and 15N chemical shift assignments of the N-terminal fragment of PaaR2 regulator encoded on the cryptic prophage CP933-P in Escherichia coli O157:H7
Deposition date:
2021-01-15
Original release date:
2022-02-25
Authors:
Prolic-Kalinsek, Marusa; Loris, Remy; Volkov, Alexander
Citation:

Citation: Prolic-Kalinsek, Marusa; Volkov, Alexander; Loris, Remy. "1H, 13C, and 15N chemical shift assignments of the N-terminal fragment of PaaR2 regulator encoded on the cryptic prophage CP933-P in Escherichia coli O157:H7"  n/a ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 74 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MQKKEIRRLRLKEWFKDKTL PPKEKSYLSQLMSGRASFGE KAARRIEQTYGMPEGYLDAE YAEQPGSSHHHHHH

Data sets:
Data typeCount
13C chemical shifts272
15N chemical shifts65
1H chemical shifts407

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PaaR21

Entities:

Entity 1, PaaR2 74 residues - Formula weight is not available

1   METGLNLYSLYSGLUILEARGARGLEUARG
2   LEULYSGLUTRPPHELYSASPLYSTHRLEU
3   PROPROLYSGLULYSSERTYRLEUSERGLN
4   LEUMETSERGLYARGALASERPHEGLYGLU
5   LYSALAALAARGARGILEGLUGLNTHRTYR
6   GLYMETPROGLUGLYTYRLEUASPALAGLU
7   TYRALAGLUGLNPROGLYSERSERHISHIS
8   HISHISHISHIS

Samples:

sample_1: PaaR2 N-terminal domain (residues 1-68), [U-13C; U-15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 65 mM; pH: 6.0; pressure: 1 atm; temperature: 298 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 - collection, processing

NMRPipe - processing

CCPN - chemical shift assignment, data analysis, peak picking

qMDD - processing

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

UNP Q8XAD6
AlphaFold Q7ADP3

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