BMRB Entry 26880

Name: 1H, 13C and 15N backbone assignments of the R3 domain of talin (residues 781-911) carrying four mutations T809I, T833V, T867V and T901I (R3-IVVI)
Published: 2018-06-26

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26880

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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 assignments of the R3 domain of talin (residues 781-911) carrying four mutations T809I, T833V, T867V and T901I (R3-IVVI)

Deposition date:

2016-08-23

Original release date:

2018-06-26

Authors:

Baxter, Nicola; Williamson, Mike; Barsukov, Igor

Citation:

Citation: Baxter, Nicola; Zacharchenko, Thomas; Barsukov, Igor; Williamson, Mike. "Pressure-Dependent Chemical Shifts in the R3 Domain of Talin Show that It Is Thermodynamically Poised for Binding to Either Vinculin or RIAM" Structure 25, 1856-11866.e2 (2017).
PubMed: 29153504

Assembly members:

Assembly members:
R3-IVVI_protein, polymer, 131 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: pET151/D-TOPO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
R3-IVVI_protein: GIDPFTAHATGAGPAGRYDQ ATDTILTVIENIFSSMGDAG EMVRQARILAQAVSDLVNAI KADAEGESDLENSRKLLSAA KILADAVAKMVEAAKGAAAH PDSEEQQQRLREAAEGLRMA INAAAQNAIKK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	392
15N chemical shifts	138
1H chemical shifts	150

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	R3-IVVI	1

Entities:

Entity 1, R3-IVVI 131 residues - Formula weight is not available

Residues 1-6 (781-786) represent a non-native affinity tag

1

GLY

ILE

ASP

PRO

PHE

THR

ALA

HIS

ALA

THR

2

GLY

ALA

GLY

PRO

ALA

GLY

ARG

TYR

ASP

GLN

3

ALA

THR

ASP

THR

ILE

LEU

THR

VAL

ILE

GLU

4

ASN

ILE

PHE

SER

MET

GLY

ASP

ALA

GLY

5

GLU

MET

VAL

ARG

GLN

ALA

ARG

ILE

LEU

ALA

6

GLN

ALA

VAL

SER

ASP

LEU

VAL

ASN

ALA

ILE

7

LYS

ALA

ASP

ALA

GLU

GLY

GLU

SER

ASP

LEU

8

GLU

ASN

SER

ARG

LYS

LEU

SER

ALA

9

LYS

ILE

LEU

ALA

ASP

ALA

VAL

ALA

LYS

MET

10

VAL

GLU

ALA

LYS

GLY

ALA

HIS

11

PRO

ASP

SER

GLU

GLN

ARG

LEU

12

ARG

GLU

ALA

GLU

GLY

LEU

ARG

MET

ALA

13

ILE

ASN

ALA

GLN

ASN

ALA

ILE

LYS

14

LYS

Samples:

sample_1: R3-IVVI protein, [U-100% 13C; U-100% 15N], 0.75 mM; sodium phosphate 20 mM; sodium chloride 150 mM; TCEP 0.5 mM; TSP, [U-2H], 0.4 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 170 mM; pH: 6.5; 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
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
2D HN(CO)CACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

Felix, Accelrys Software Inc. - chemical shift assignment, data analysis, processing

NMR spectrometers:

Bruker Avance 800 MHz
Bruker DRX 500 MHz

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