BMRB Entry 34926

Name: helix shuffled variant of domain B pf protein A
Published: 2025-02-04

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PDB ID: 9fzm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34926
MolProbity Validation Chart

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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:

helix shuffled variant of domain B pf protein A

Deposition date:

2024-07-05

Original release date:

2025-02-04

Authors:

Weininger, U.; Bobolowski, H.

Citation:

Citation: Bobolowski, H.; Fiedler, E.; Haupts, U.; Lilie, H.; Weininger, U.. "A functional helix shuffled variant of the B domain of Staphylococcus aureus" Protein Sci. 34, e70012-e70012 (2025).
PubMed: 39840789

Assembly members:

Assembly members:
entity_1, polymer, 63 residues, 7011.666 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: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ADNKFSQSANLLAEAKKLND AQGGITEEQRNGFIQSLKDD AKTNPGNNKEQQNAFYEILH LPK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	193
15N chemical shifts	60
1H chemical shifts	397

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 63 residues - 7011.666 Da.

1

ALA

ASP

ASN

LYS

PHE

SER

GLN

SER

ALA

ASN

2

LEU

ALA

GLU

ALA

LYS

LEU

ASN

ASP

3

ALA

GLN

GLY

ILE

THR

GLU

GLN

ARG

4

ASN

GLY

PHE

ILE

GLN

SER

LEU

LYS

ASP

5

ALA

LYS

THR

ASN

PRO

GLY

ASN

LYS

GLU

6

GLN

ASN

ALA

PHE

TYR

GLU

ILE

LEU

HIS

7

LEU

PRO

LYS

Samples:

sample_1: B domain of protein A, [U-100% 13C; U-100% 15N], 0.5 mM; NaCl 137 mM; KCl 2.7 mM; Na2HPO4 8 mM; KH2PO4 2 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 bar; temperature: 288.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

NMRViewJ, Johnson - chemical shift assignment, peak picking

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

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

TALOS+, Cornilescu - geometry optimization

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker AVANCE III 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks