BMRB Entry 27272

Name: Backbone assignment of SGTA C-terminal domain
Published: 2018-06-19

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27272

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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 C-terminal domain

Deposition date:

2017-10-04

Original release date:

2018-06-19

Authors:

Martinez Lumbreras, Santiago; 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_Cter, polymer, 103 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_Cter: GSTGGVGSFDIAGLLNNPGF MSMASNLMNNPQIQQLMSGM ISGGNNPLGTPGTSPSQNDL ASLIQAGQQFAQQMQQQNPE LIEQLRSQIRSRTPSASNDD QQE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	173
15N chemical shifts	53
1H chemical shifts	68

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SGTA_Cter	1

Entities:

Entity 1, SGTA_Cter 103 residues - Formula weight is not available

1

GLY

SER

THR

GLY

VAL

GLY

SER

PHE

ASP

2

ILE

ALA

GLY

LEU

ASN

PRO

GLY

PHE

3

MET

SER

MET

ALA

SER

ASN

LEU

MET

ASN

4

PRO

GLN

ILE

GLN

LEU

MET

SER

GLY

MET

5

ILE

SER

GLY

ASN

PRO

LEU

GLY

THR

6

PRO

GLY

THR

SER

PRO

SER

GLN

ASN

ASP

LEU

7

ALA

SER

LEU

ILE

GLN

ALA

GLY

GLN

PHE

8

ALA

GLN

MET

GLN

ASN

PRO

GLU

9

LEU

ILE

GLU

GLN

LEU

ARG

SER

GLN

ILE

ARG

10

SER

ARG

THR

PRO

SER

ALA

SER

ASN

ASP

11

GLN

GLU

Samples:

Cter_CND: SGTA_Cter, [U-13C; U-15N; U-2H], 300 uM; potassium phosphate 10 mM; sodium chloride 100 mM; TCEP 250 uM; DDM 0.025%

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	Cter_CND	isotropic	sample_conditions_1
3D CBCA(CO)NH	Cter_CND	isotropic	sample_conditions_1
3D HNCACB	Cter_CND	isotropic	sample_conditions_1
3D HNCO	Cter_CND	isotropic	sample_conditions_1
3D HN(CA)CO	Cter_CND	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 950 MHz

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