BMRB Entry 31031

Title:
NMR Structure of Streptococcal Protein GB1 Backbone Modified Variant: beta-ACPC24, beta-3-Lys28, beta-3-Lys31, beta-ACPC35
Deposition date:
2022-06-29
Original release date:
2022-11-17
Authors:
Rao, S.; Reinert, Z.
Citation:

Citation: Rao, S.; Harmon, T.; Heath, S.; Wolfe, J.; Santhouse, J.; O'Brien, G.; Distefano, A.; Reinert, Z.; Horne, W.. "Chemical Shifts of Artificial Monomers Used to Construct Heterogeneous-Backbone Protein Mimetics in Random Coil and Folded States"  to be published ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 57 residues, 6246.825 Da.

Natural source:

Natural source:   Common Name: Streptococcus   Taxonomy ID: 1301   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus not available

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Data sets:
Data typeCount
1H chemical shifts388

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 57 residues - 6246.825 Da.

1   ASPTHRTYRLYSLEUILELEUASNGLYLYS
2   THRLEULYSGLYGLUTHRTHRTHRGLUALA
3   VALASPALAXCPTHRALAGLUB3KVALPHE
4   B3KGLNTYRALAXCPASPASNGLYVALASP
5   GLYGLUTRPTHRTYRASPASPALATHRLYS
6   THRPHETHRVALTHRGLUNH2

Samples:

sample_1: Immunoglobulin G-binding protein G 0.65 mM; sodium phosphate 20 mM; DSS 0.1 mM

sample_conditions_1: ionic strength: 40 mM; pH: 7 pH*; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

TopSpin, Bruker Biospin - processing

NMRFAM-SPARKY, Lee, Tonelli, Markley - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 700 MHz