BMRB Entry 31115

Name: Site-specific Aspartic Acid Dehydration and Isomerization in Streptococcal Protein GB1: D-Asp40 Variant
Published: 2024-04-23

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PDB ID: 8um9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31115
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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):

Entity Sequences (FASTA):
entity_1: MQYKLILNGKTLKGETTTEA VDAATAEKVFKQYANDNGVX GEWTYDDATKTFTVTE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
1H chemical shifts	386

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 56 residues - 6228.809 Da.

1

MET

GLN

TYR

LYS

LEU

ILE

LEU

ASN

GLY

LYS

2

THR

LEU

LYS

GLY

GLU

THR

GLU

ALA

3

VAL

ASP

ALA

THR

ALA

GLU

LYS

VAL

PHE

4

LYS

GLN

TYR

ALA

ASN

ASP

ASN

GLY

VAL

DAS

5

GLY

GLU

TRP

THR

TYR

ASP

ALA

THR

LYS

6

THR

PHE

THR

VAL

THR

GLU

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:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_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