BMRB Entry 27275

Name: Backbone assignment of SGTA TPR_C-terminal(deltaQ) domains
Published: 2018-06-19

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27275

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Backbone assignment of SGTA TPR_C-terminal(deltaQ) domains PubMed: 29996828

Deposition date: 2017-10-05 Original release date: 2018-06-19

Authors: Martinez Lumbreras, Santiago; Thapaliya, Arjun; Isaacson, Rivka

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).

Assembly members:
SGTA_TPR-NNP, polymer, 192 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
SGTA_TPR-NNP: GSEEDSAEAERLKTEGNEQM KVENFEAAVHFYGKAIELNP ANAVYFCNRAAAYSKLGNYA GAVQDCERAICIDPAYSKAY GRMGLALSSLNKHVEAVAYY KKALELDPDNETYKSNLKIA ELKLREAPSPTGGVGSFDIA GLLNNPGFMSMASNLMNNPQ IQQLMSGMISGGNNPLGTPG TSPSQNDLASLI

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	462
15N chemical shifts	152
1H chemical shifts	152

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SGTA_TPR-NNP	1

Entities:

Entity 1, SGTA_TPR-NNP 192 residues - Formula weight is not available

1

GLY

SER

GLU

ASP

SER

ALA

GLU

ALA

GLU

2

ARG

LEU

LYS

THR

GLU

GLY

ASN

GLU

GLN

MET

3

LYS

VAL

GLU

ASN

PHE

GLU

ALA

VAL

HIS

4

PHE

TYR

GLY

LYS

ALA

ILE

GLU

LEU

ASN

PRO

5

ALA

ASN

ALA

VAL

TYR

PHE

CYS

ASN

ARG

ALA

6

ALA

TYR

SER

LYS

LEU

GLY

ASN

TYR

ALA

7

GLY

ALA

VAL

GLN

ASP

CYS

GLU

ARG

ALA

ILE

8

CYS

ILE

ASP

PRO

ALA

TYR

SER

LYS

ALA

TYR

9

GLY

ARG

MET

GLY

LEU

ALA

LEU

SER

LEU

10

ASN

LYS

HIS

VAL

GLU

ALA

VAL

ALA

TYR

11

LYS

ALA

LEU

GLU

LEU

ASP

PRO

ASP

ASN

12

GLU

THR

TYR

LYS

SER

ASN

LEU

LYS

ILE

ALA

13

GLU

LEU

LYS

LEU

ARG

GLU

ALA

PRO

SER

PRO

14

THR

GLY

VAL

GLY

SER

PHE

ASP

ILE

ALA

15

GLY

LEU

ASN

PRO

GLY

PHE

MET

SER

16

MET

ALA

SER

ASN

LEU

MET

ASN

PRO

GLN

17

ILE

GLN

LEU

MET

SER

GLY

MET

ILE

SER

18

GLY

ASN

PRO

LEU

GLY

THR

PRO

GLY

19

THR

SER

PRO

SER

GLN

ASN

ASP

LEU

ALA

SER

20

LEU

ILE

Samples:

sample_1: SGTA_TPR-NNP, [U-100% 13C; U-100% 15N], 900 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	sample_1	isotropic	sample_conditions_1
3D HNCA	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 shifts
SPARKY: Backbone or all simulated shifts