BMRB Entry 18691

Name: Backbone 1H, 13C, and 15N backbone resonance assignments of the TPR1 domain of mouse STI1
Published: 2012-10-18

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18691

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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 1H, 13C, and 15N backbone resonance assignments of the TPR1 domain of mouse STI1

Deposition date:

2012-08-30

Original release date:

2012-10-18

Authors:

Maciejewski, Andrzej; Choy, Wing-Yiu

Citation:

Citation: Maciejewski, Andrzej; Prado, Marco; Choy, Wing-Yiu. "1H, 15N, and 13C backbone resonance assignments of the TPR1 and TPR2A domains of mouse STI1." Biomol. NMR Assignments 7, 305-310 (2013).
PubMed: 23070844

Assembly members:

Assembly members:
tpr1, polymer, 118 residues, Formula weight is not available

Natural source:

Natural source: Common Name: House 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):
tpr1: GEQVNELKEKGNKALSAGNI DDALQCYSEAIKLDPQNHVL YSNRSAAYAKKGDYQKAYED GCKTVDLKPDWGKGYSRKAA ALEFLNRFEEAKRTYEEGLK HEANNLQLKEGLQNMEAR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	198
15N chemical shifts	111
1H chemical shifts	111

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	tpr1	1

Entities:

Entity 1, tpr1 118 residues - Formula weight is not available

1

GLY

GLU

GLN

VAL

ASN

GLU

LEU

LYS

GLU

LYS

2

GLY

ASN

LYS

ALA

LEU

SER

ALA

GLY

ASN

ILE

3

ASP

ALA

LEU

GLN

CYS

TYR

SER

GLU

ALA

4

ILE

LYS

LEU

ASP

PRO

GLN

ASN

HIS

VAL

LEU

5

TYR

SER

ASN

ARG

SER

ALA

TYR

ALA

LYS

6

LYS

GLY

ASP

TYR

GLN

LYS

ALA

TYR

GLU

ASP

7

GLY

CYS

LYS

THR

VAL

ASP

LEU

LYS

PRO

ASP

8

TRP

GLY

LYS

GLY

TYR

SER

ARG

LYS

ALA

9

ALA

LEU

GLU

PHE

LEU

ASN

ARG

PHE

GLU

10

ALA

LYS

ARG

THR

TYR

GLU

GLY

LEU

LYS

11

HIS

GLU

ALA

ASN

LEU

GLN

LEU

LYS

GLU

12

GLY

LEU

GLN

ASN

MET

GLU

ALA

ARG

Samples:

sample_1: sodium phosphate 50 mM; sodium chloride 50 mM; DTT 1 mM; DSS 100 uM; tpr1, [U-13C; U-15N], 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 273 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
3D C(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

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

SPARKY, Goddard - data analysis

NMR spectrometers:

Varian INOVA 600 MHz

PDB	1ELW
REF	XP_004713702