BMRB Entry 31115

Title:
Site-specific Aspartic Acid Dehydration and Isomerization in Streptococcal Protein GB1: D-Asp40 Variant
Deposition date:
2023-10-17
Original release date:
2024-04-23
Authors:
Heath, S.; Guseman, A.; Gronenborn, A.; Horne, W.
Citation:

Citation: Heath, S.; Guseman, A.; Gronenborn, A.; Horne, W.. "Effects of Site-Specific Aspartic Acid Dehydration and Isomerization on the Folded Structure and Stability of Protein GB1"  To be published ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 56 residues, 6228.809 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 shifts386

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 56 residues - 6228.809 Da.

1   METGLNTYRLYSLEUILELEUASNGLYLYS
2   THRLEULYSGLYGLUTHRTHRTHRGLUALA
3   VALASPALAALATHRALAGLULYSVALPHE
4   LYSGLNTYRALAASNASPASNGLYVALDAS
5   GLYGLUTRPTHRTYRASPASPALATHRLYS
6   THRPHETHRVALTHRGLU

Samples:

sample_1: B1 Domain of Streptococcal Protein G, D-Asp40 Variant 0.12 mM; sodium phosphate 20 mM; DSS 0.1 mM

sample_conditions_1: ionic strength: 41 mM; pH: 7 pH*; pressure: 1 atm; temperature: 298 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

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

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

NMR spectrometers:

  • Bruker AVANCE III 700 MHz