BMRB Entry 31162

Title:
Backbone Modification in the GA Module of Protein PAB: ACPC residues at positions 5 and 13, beta3 residue at position 9
Deposition date:
2024-04-05
Original release date:
2024-05-31
Authors:
Lin, Y.; Horne, W.
Citation:

Citation: Lin, Y.; Horne, W.. "Backbone Modification in a Protein Hydrophobic Core"  Chemistry ., .-. (2024).
PubMed: 38753977

Assembly members:

Assembly members:
entity_1, polymer, 48 residues, 5158.899 Da.

Natural source:

Natural source:   Common Name: Finegoldia magna   Taxonomy ID: 1260   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Finegoldia magna

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: LKNAXEDAXAELXKAGITSD FYFNAINKAKTVEEVNALKN EILKAHAX

Data sets:
Data typeCount
1H chemical shifts345

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 48 residues - 5158.899 Da.

1   LEULYSASNALAXCPGLUASPALABILALA
2   GLULEUXCPLYSALAGLYILETHRSERASP
3   PHETYRPHEASNALAILEASNLYSALALYS
4   THRVALGLUGLUVALASNALALEULYSASN
5   GLUILELEULYSALAHISALANH2

Samples:

sample_1: GA Module of Protein PAB: ACPC residues at positions 5 and 13, beta3 residue at position 9 1 mM; dss 0.2 mM

sample_conditions_1: ionic strength: 1 mM; pH: 5.8 pH*; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - processing

Poky, Manthey, Tonelli, Clos II, Rahimi, Markley and Lee - data analysis

ARIA, Linge, O'Donoghue and Nilges - refinement, structure calculation

NMR spectrometers:

  • Bruker AVANCE 700 MHz