BMRB Entry 26920

Name: 1H, 13C and 15N backbone resonance assignment of the TPR2B domain of mouse STI1
Published: 2017-08-11

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26920

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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:

1H, 13C and 15N backbone resonance assignment of the TPR2B domain of mouse STI1

Deposition date:

2016-10-19

Original release date:

2017-08-11

Authors:

Choy, Wing-Yiu; Maciejewski, Andrzej; Prado, Marco

Citation:

Citation: Maciejewski, Andrzej; Prado, Vania; Prado, Marco; Choy, Wing-Yiu. "Molecular basis for the interaction between stress-inducible phosphoprotein 1 (STIP1) and S100A1" Biochem. J. 474, 1853-1866 (2017).
PubMed: 28408431

Assembly members:

Assembly members:
TPR2B, polymer, 137 residues, 15795.8 Da.

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pDEST17

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TPR2B: GQERLAYINPDLALEEKNKG NECFQKGDYPQAMKHYTEAI KRNPRDAKLYSNRAACYTKL LEFQLALKDCEECIQLEPTF IKGYTRKAAALEAMKDYTKA MDVYQKALDLDSSCKEAADG YQRCMMAQYNRHDSPED

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	247
15N chemical shifts	122
1H chemical shifts	122

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TPR2B	1

Entities:

Entity 1, TPR2B 137 residues - 15795.8 Da.

N-terminal glycine is a non-native residue from a TEV recognition site

1

GLY

GLN

GLU

ARG

LEU

ALA

TYR

ILE

ASN

PRO

2

ASP

LEU

ALA

LEU

GLU

LYS

ASN

LYS

GLY

3

ASN

GLU

CYS

PHE

GLN

LYS

GLY

ASP

TYR

PRO

4

GLN

ALA

MET

LYS

HIS

TYR

THR

GLU

ALA

ILE

5

LYS

ARG

ASN

PRO

ARG

ASP

ALA

LYS

LEU

TYR

6

SER

ASN

ARG

ALA

CYS

TYR

THR

LYS

LEU

7

LEU

GLU

PHE

GLN

LEU

ALA

LEU

LYS

ASP

CYS

8

GLU

CYS

ILE

GLN

LEU

GLU

PRO

THR

PHE

9

ILE

LYS

GLY

TYR

THR

ARG

LYS

ALA

10

LEU

GLU

ALA

MET

LYS

ASP

TYR

THR

LYS

ALA

11

MET

ASP

VAL

TYR

GLN

LYS

ALA

LEU

ASP

LEU

12

ASP

SER

CYS

LYS

GLU

ALA

ASP

GLY

13

TYR

GLN

ARG

CYS

MET

ALA

GLN

TYR

ASN

14

ARG

HIS

ASP

SER

PRO

GLU

ASP

Samples:

sample_1: TPR2B, [U-99% 13C; U-99% 15N], 500 uM; sodium phosphate 50 mM; sodium chloride 50 mM; DTT 1 mM; DSS 100 uM

sample_conditions_1: ionic strength: 150 mM; pH: 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 HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

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

VNMRJ, Varian - collection

NMR spectrometers:

Varian INOVA 600 MHz

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