BMRB Entry 27276

Name: Backbone assignment of SGTA N-terminal domain including linker residues
Published: 2018-06-19

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27276

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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:

Backbone assignment of SGTA N-terminal domain including linker residues

Deposition date:

2017-10-05

Original release date:

2018-06-19

Authors:

Martinez Lumbreras, Santiago; Krysztofinska, Ewelina; Isaacson, Rivka

Citation:

Citation: Martinez-Lumbreras, Santiago; Krysztofinska, Ewelina; Thapaliya, Arjun; Spilotros, Alessandro; Matak-Vinkovic, Dijana; Salvadori, Enrico; Roboti, Peristera; Nyathi, Yvonne; Muench, Janina; Roessler, Maxie; Svergun, Dmitri; High, Stephen; Isaacson, Rivka. "Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control" BMC Biol. 16, 76-76 (2018).
PubMed: 29996828

Assembly members:

Assembly members:
SGTA_Nter_linker, polymer, 88 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28_Txr_6xH_TEV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SGTA_Nter_linker: GSMDNKKRLAYAIIQFLHDQ LRHGGLSSDAQESLEVAIQC LETAFGVTVEDSDLALPQTL PEIFEAAATGKEMPQDLRSP ARTPPSEE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	246
15N chemical shifts	87
1H chemical shifts	94

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SGTA_Nter-linker	1

Entities:

Entity 1, SGTA_Nter-linker 88 residues - Formula weight is not available

1

GLY

SER

MET

ASP

ASN

LYS

ARG

LEU

ALA

2

TYR

ALA

ILE

GLN

PHE

LEU

HIS

ASP

GLN

3

LEU

ARG

HIS

GLY

LEU

SER

ASP

ALA

4

GLN

GLU

SER

LEU

GLU

VAL

ALA

ILE

GLN

CYS

5

LEU

GLU

THR

ALA

PHE

GLY

VAL

THR

VAL

GLU

6

ASP

SER

ASP

LEU

ALA

LEU

PRO

GLN

THR

LEU

7

PRO

GLU

ILE

PHE

GLU

ALA

THR

GLY

8

LYS

GLU

MET

PRO

GLN

ASP

LEU

ARG

SER

PRO

9

ALA

ARG

THR

PRO

SER

GLU

Samples:

sample_1: SGTA_Nter_linker, [U-100% 13C; U-100% 15N], 800 uM; potassium phosphate 10 mM; sodium chloride 100 mM; TCEP 250 uM

sample_conditions_1: ionic strength: 130 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	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:

TOPSPIN, Bruker Biospin - collection

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

CCPN_Analysis, CCPN - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz

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