BMRB Entry 30389

Name: Solution structure of AGL55
Published: 2019-01-11

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PDB ID: 6bzj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30389
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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:

Solution structure of AGL55

Deposition date:

2017-12-24

Original release date:

2019-01-11

Authors:

Qiu, C.; Yuan, Y.; Castellino, F.

Citation:

Citation: Qiu, Cunjia; Yuan, Yue; Zajicek, Jaroslav; Liang, Zhong; Balsara, Rashna; Brito-Robionson, Teresa; Lee, Shaun; Ploplis, Victoria; Castellino, Francis. "Contributions of different modules of the plasminogen-binding Streptococcus pyogenes M-protein that mediate its functional dimerization" J. Struct. Biol. 204, 151-164 (2018).
PubMed: 30071314

Assembly members:

Assembly members:
entity_1, polymer, 57 residues, 6742.396 Da.

Natural source:

Natural source: Common Name: Streptococcus pyogenes Taxonomy ID: 1138874 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptococcus pyogenes

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli DH5[alpha] Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSAGLQEKERELEDLKDAEL KRLNEERHDHDKREAERKAL EDKLADKQEHLDGALRY

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	236
15N chemical shifts	54
1H chemical shifts	363

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 57 residues - 6742.396 Da.

1

GLY

SER

ALA

GLY

LEU

GLN

GLU

LYS

GLU

ARG

2

GLU

LEU

GLU

ASP

LEU

LYS

ASP

ALA

GLU

LEU

3

LYS

ARG

LEU

ASN

GLU

ARG

HIS

ASP

HIS

4

ASP

LYS

ARG

GLU

ALA

GLU

ARG

LYS

ALA

LEU

5

GLU

ASP

LYS

LEU

ALA

ASP

LYS

GLN

GLU

HIS

6

LEU

ASP

GLY

ALA

LEU

ARG

TYR

Samples:

sample_1: BisTris-d19, [U-99% 2H], 20 mM; DSS 1 mM; sodium azide 1 mM; EDTA 1 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D NOESY-HSQC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, data analysis, processing

SPARKY, Goddard - chemical shift assignment, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

Bruker AvanceII 800 MHz

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