BMRB Entry 34430

Name: NMR solution structure of staphylococcal protein A, C domain
Published: 2020-09-07

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34430

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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: NMR solution structure of staphylococcal protein A, C domain

Deposition date: 2019-08-30 Original release date: 2020-09-07

Authors: Backlund, S.; Iwai, H.

Citation: Backlund, S.; Iwai, H.. "NMR solution structure of staphylococcal protein A, C domain" . ., .-..

Assembly members:
entity_1, polymer, 58 residues, 6653.353 Da.

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

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):
entity_1: SDNKFNKEQQNAFYEILHLP NLTEEQRNGFIQSLKDDPSV SKEILAEAKKLNDAQAPK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	272
15N chemical shifts	68
1H chemical shifts	418

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 - 6653.353 Da.

1

SER

ASP

ASN

LYS

PHE

ASN

LYS

GLU

GLN

2

ASN

ALA

PHE

TYR

GLU

ILE

LEU

HIS

LEU

PRO

3

ASN

LEU

THR

GLU

GLN

ARG

ASN

GLY

PHE

4

ILE

GLN

SER

LEU

LYS

ASP

PRO

SER

VAL

5

SER

LYS

GLU

ILE

LEU

ALA

GLU

ALA

LYS

6

LEU

ASN

ASP

ALA

GLN

ALA

PRO

LYS

Samples:

sample_1: Protein A C domain, [U-20% 13C; U-100% 15N], 5.6 mM

sample_2: Protein A C domain, [U-20% 13C; U-100% 15N], 2.8 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6; pressure: 1 atm; temperature: 303 K

sample_conditions_2: ionic strength: 20 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_2
3D HNCA	sample_1	isotropic	sample_conditions_1
2D CACO	sample_2	isotropic	sample_conditions_2
2D CON	sample_2	isotropic	sample_conditions_2
3D HCCH-COSY	sample_2	isotropic	sample_conditions_2
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_2
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_2
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
3D HNCACBi	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCOi	sample_1	isotropic	sample_conditions_1
2D CACO	sample_1	isotropic	sample_conditions_1
2D CON	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1

Software:

CcpNmr Analysis v2.4.2, CCPN - chemical shift assignment, peak picking

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation

Amber v14, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

PSVS v1.5, Bhattacharya and Montelione - data analysis

TALOS vN, Cornilescu, Delaglio and Bax - chemical shift assignment

NMR spectrometers:

Bruker AVANCE 850 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts