BMRB Entry 16163

Name: NMR structure of the N-terminal domain of kindlin1
Published: 2009-12-01

Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16163

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

NMR structure of the N-terminal domain of kindlin1

Deposition date:

2009-02-09

Original release date:

2009-12-01

Authors:

Goult, Benjamin

Citation:

Citation: Goult, Benjamin; Bouaouina, Mohamed; Harburger, David; Bate, Neil; Patel, Bipin; Anthis, Nicholas; Campbell, Iain; Calderwood, David; Barsukov, Igor; Roberts, Gordon; Critchley, David. "The structure of the N-terminus of kindlin-1: a domain important for alphaiibbeta3 integrin activation." J. Mol. Biol. 394, 944-956 (2009).
PubMed: 19804783

Assembly members:

Assembly members:
F0, polymer, 102 residues, Formula weight is not available

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: pET-151

Entity Sequences (FASTA):

Entity Sequences (FASTA):
F0: GIDPFTMLSSGDLTSASWEL VVRVDHANGEQQTEITLRVS GDLHIGGVMLKLVEQMNIAQ DWSDYALWWEQKRCWLLKTH WTLDKCGVQADANLLFTPQH KM

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	442
15N chemical shifts	118
1H chemical shifts	720

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	F0	1

Entities:

Entity 1, F0 102 residues - Formula weight is not available

Residues -5 to 0 represent a non-native affinity tag

1

GLY

ILE

ASP

PRO

PHE

THR

MET

LEU

SER

2

GLY

ASP

LEU

THR

SER

ALA

SER

TRP

GLU

LEU

3

VAL

ARG

VAL

ASP

HIS

ALA

ASN

GLY

GLU

4

GLN

THR

GLU

ILE

THR

LEU

ARG

VAL

SER

5

GLY

ASP

LEU

HIS

ILE

GLY

VAL

MET

LEU

6

LYS

LEU

VAL

GLU

GLN

MET

ASN

ILE

ALA

GLN

7

ASP

TRP

SER

ASP

TYR

ALA

LEU

TRP

GLU

8

GLN

LYS

ARG

CYS

TRP

LEU

LYS

THR

HIS

9

TRP

THR

LEU

ASP

LYS

CYS

GLY

VAL

GLN

ALA

10

ASP

ALA

ASN

LEU

PHE

THR

PRO

GLN

HIS

11

LYS

MET

Samples:

15N: F0, [U-100% 15N], 200 ± 5 uM; DTT 2 ± 0.1 mM; sodium phosphate 20 ± 0.3 mM; sodium chloride 50 ± 0.3 mM; H2O 90%; D2O 10%

double: F0, [U-100% 13C; U-100% 15N], 200 ± 5 uM; DTT 2 ± 0.1 mM; sodium phosphate 20 ± 0.3 mM; sodium chloride 50 ± 0.3 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	15N	isotropic	sample_conditions_1
2D 1H-13C HSQC	double	isotropic	sample_conditions_1
3D HNCO	double	isotropic	sample_conditions_1
3D HNCA	double	isotropic	sample_conditions_1
3D HNCACB	double	isotropic	sample_conditions_1
3D HCCH-TOCSY	double	isotropic	sample_conditions_1
3D 1H-15N NOESY	15N	isotropic	sample_conditions_1
3D 1H-13C NOESY	double	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - peak picking, structure solution

ANALYSIS v1.15, CCPN - chemical shift assignment, data analysis, peak picking

ARIA v1.2, Linge, O'Donoghue and Nilges - refinement, structure solution

NMR spectrometers:

Bruker DRX 600 MHz
Bruker DRX 600 MHz
Bruker DRX 800 MHz

PDB	2KMC
DBJ	BAC34417
GB	EDL28367 EDL28368
REF	NP_932146
SP	P59113
AlphaFold	P59113