BMRB Entry 31012

Name: Backbone-modified variant of the B domain of Staphylococcal protein A: beta3- and ACPC-residues in helix 2
Published: 2023-04-25

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PDB ID: 7urj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31012
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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:

Backbone-modified variant of the B domain of Staphylococcal protein A: beta3- and ACPC-residues in helix 2

Deposition date:

2022-04-22

Original release date:

2023-04-25

Authors:

Santhouse, J.; Leung, J.; Chong, L.; Horne, W.

Citation:

Citation: Santhouse, J.; Leung, J.; Chong, L.; Horne, W.. "Effects of Altered Backbone Composition on Protein Folded States, Unfolded States, and Folding Energetics: Integration of Simulation and Experiment" .

Assembly members:

Assembly members:
entity_1, polymer, 59 residues, 6610.357 Da.

Natural source:

Natural source: Common Name: Staphylococcus aureus Taxonomy ID: 1280 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ADNKFNKEQQNAFYEILHLP NLNEXQRNAFIXSLKDDPSQ SANLLAEAKKLNDAQAPKX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
1H chemical shifts	434

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 59 residues - 6610.357 Da.

1

ALA

ASP

ASN

LYS

PHE

ASN

LYS

GLU

GLN

2

ASN

ALA

PHE

TYR

GLU

ILE

LEU

HIS

LEU

PRO

3

ASN

LEU

ASN

GLU

XCP

GLN

ARG

B3X

ALA

PHE

4

ILE

XCP

SER

LEU

B3K

ASP

PRO

SER

GLN

5

SER

ALA

ASN

LEU

ALA

GLU

ALA

LYS

6

LEU

ASN

ASP

ALA

GLN

ALA

PRO

LYS

NH2

Samples:

sample_1: entity_1 1.4 mM; DSS 0.2 mM

sample_conditions_1: ionic strength: 10 mM; pH: 5 pH*; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	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 700 MHz