BMRB Entry 34975

Name: CS-ROSETTA Structure of the Z Domain of the IgG-Binding Staphylococcal Protein A
Published: 2026-01-18

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PDB ID: 9hxs
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34975
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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:

CS-ROSETTA Structure of the Z Domain of the IgG-Binding Staphylococcal Protein A

Deposition date:

2025-01-08

Original release date:

2026-01-18

Authors:

Goodman, J.; Nagy, T.; Jonsson, M.; Moller, M.; Hober, S.; Wolf-Watz, M.

Citation:

Citation: Goodman, J.; Nagy, T.; Jonsson, M.; Moller, M.; Hober, S.; Wolf-Watz, M.. "CS-ROSETTA Structure of the Z Domain of the IgG-Binding Staphylococcal Protein A" .

Assembly members:

Assembly members:
entity_1, polymer, 58 residues, 6648.316 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: VDNKFNKEQQNAFYEILHLP NLNEEQRNAFIQSLKDDPSQ SANLLAEAKKLNDAQAPK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	153
15N chemical shifts	51
1H chemical shifts	51

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 58 residues - 6648.316 Da.

1

VAL

ASP

ASN

LYS

PHE

ASN

LYS

GLU

GLN

2

ASN

ALA

PHE

TYR

GLU

ILE

LEU

HIS

LEU

PRO

3

ASN

LEU

ASN

GLU

GLN

ARG

ASN

ALA

PHE

4

ILE

GLN

SER

LEU

LYS

ASP

PRO

SER

GLN

5

SER

ALA

ASN

LEU

ALA

GLU

ALA

LYS

6

LEU

ASN

ASP

ALA

GLN

ALA

PRO

LYS

Samples:

sample_1: Protein Z, [U-100% 13C; U-100% 15N], 2 mg/mL; MES 25 mM; CaCl2 1 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6; pressure: 1 bar; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

CS-ROSETTA, Shen, Vernon, Baker and Bax - refinement, structure calculation

CcpNmr Analysis Assign, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

Bruker AVANCE NEO 850 MHz

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