BMRB Entry 17206

Name: villin head piece domain of human ABLIM2
Published: 2010-10-22

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17206

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:

villin head piece domain of human ABLIM2

Deposition date:

2010-09-24

Original release date:

2010-10-22

Authors:

Bruton, Shaun; Pfuhl, Mark

Citation:

Citation: Bruton, Shaun; Pfuhl, Mark. "Solution NMR study of the actin binding domain of ABLIM2" .

Assembly members:

Assembly members:
VHD, polymer, 67 residues, 8212.633 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pLEICS-07

Entity Sequences (FASTA):

Entity Sequences (FASTA):
VHD: QYKIYPYDSLIVTNRIRVKL PKDVDRTRLERHLSPEEFQE VFGMSIEEFDRLALWKRNDL KKKALLF

Data sets:

assigned_chemical_shifts
- ShiftList1

Data type	Count
13C chemical shifts	331
15N chemical shifts	68
1H chemical shifts	529

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	VHD in monomer	1

Entities:

Entity 1, VHD in monomer 67 residues - 8212.633 Da.

1

GLN

TYR

LYS

ILE

TYR

PRO

TYR

ASP

SER

LEU

2

ILE

VAL

THR

ASN

ARG

ILE

ARG

VAL

LYS

LEU

3

PRO

LYS

ASP

VAL

ASP

ARG

THR

ARG

LEU

GLU

4

ARG

HIS

LEU

SER

PRO

GLU

PHE

GLN

GLU

5

VAL

PHE

GLY

MET

SER

ILE

GLU

PHE

ASP

6

ARG

LEU

ALA

LEU

TRP

LYS

ARG

ASN

ASP

LEU

7

LYS

ALA

LEU

PHE

Samples:

sample_1: VHD 0.7 ± 0.02 mM; sodium phosphate 20 ± 0.1 mM; sodium chloride 50 ± 0.1 mM; DTT 2 ± 0.1 mM; sodium azide 0.02 ± 0.0005 %; D2O 100%

sample_2: VHD, [U-99% 15N], 0.7 ± 0.02 mM; sodium phosphate 20 ± 0.1 mM; sodium chloride 50 ± 0.1 mM; DTT 2 ± 0.1 mM; sodium azide 0.02 ± 0.0005 %; D2O 5%; H2O 95%

sample_3: VHD, [U-99% 13C; U-99% 15N], 0.7 ± 0.02 mM; sodium phosphate 20 ± 0.1 mM; sodium chloride 50 ± 0.1 mM; DTT 2 ± 0.1 mM; sodium azide 0.02 ± 0.0005 %; D2O 5%; H2O 95%

sample_4: VHD, [U-99% 13C; U-99% 15N], 0.7 ± 0.02 mM; sodium phosphate 20 ± 0.1 mM; sodium chloride 50 ± 0.1 mM; DTT 2 ± 0.1 mM; sodium azide 0.02 ± 0.0005 %; D2O 100%

sample_conditions_1: ionic strength: 90 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_1
3D HNCACO	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_3	isotropic	sample_conditions_1
2D NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_4	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_4	isotropic	sample_conditions_1
2D 13C CT-HSQC	sample_4	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CCPN_Analysis v2.1, CCPN (Laue et al.) - chemical shift assignment, peak picking

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

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2L3X
DBJ	BAB47437 BAC04414 BAC04427 BAC32651 BAC32905
EMBL	CAD38885 CAG28314 CAG28315 CAG38375 CAG38376
GB	AAI22568 AAI41126 AAI56705 AAP23233 ABD83328
REF	NP_001001514 NP_001123555 NP_001123556 NP_001123557 NP_001123558
SP	Q6H8Q1 Q6KC51 Q8BL65
AlphaFold	Q6H8Q1 Q6KC51 Q8BL65