BMRB Entry 30390

Name: Solution structure of KTI55
Published: 2019-01-11

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PDB ID: 6bzk
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30390
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of KTI55

Deposition date: 2017-12-24 Original release date: 2019-01-11

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

Citation: Castellino, F.; Yuan, Y.; Qiu, C.; Yuan, Y.; Castellino, F.. "Solution structure of truncated PAM" . ., .-..

Assembly members:
entity_1, polymer, 57 residues, 6799.461 Da.

Natural source: Common Name: Streptococcus pyogenes Taxonomy ID: 1314 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptococcus pyogenes

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

Entity Sequences (FASTA):
entity_1: GSKTIQEKEQELKNLKDNVE LERLKNERHDHDEEAERKAL EDKLADKQEHLDGALRY

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	239
15N chemical shifts	55
1H chemical shifts	354

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 - 6799.461 Da.

1

GLY

SER

LYS

THR

ILE

GLN

GLU

LYS

GLU

GLN

2

GLU

LEU

LYS

ASN

LEU

LYS

ASP

ASN

VAL

GLU

3

LEU

GLU

ARG

LEU

LYS

ASN

GLU

ARG

HIS

ASP

4

HIS

ASP

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