BMRB Entry 50754

Name: Backbone and side-chain resonance assignments of the A2 domain of mouse von Willebrand factor
Published: 2021-08-10

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50754

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:

Backbone and side-chain resonance assignments of the A2 domain of mouse von Willebrand factor

Deposition date:

2021-02-08

Original release date:

2021-08-10

Authors:

Morimoto, Daichi; Osugi, Masanori; Mahana, Yutaka; Walinda, Erik; Shirakawa, Masahiro; Sugase, Kenji

Citation:

Citation: Morimoto, Daichi; Osugi, Masanori; Mahana, Yutaka; Walinda, Erik; Shirakawa, Masahiro; Sugase, Kenji. "Backbone resonance assignments of the A2 domain of mouse von Willebrand factor" Biomol. NMR Assignments 15, 427-431 (2021).
PubMed: 34286417

Assembly members:

Assembly members:
entity_1, polymer, 182 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: pGEX-6p-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPLGSMVLDVVFVLEGSDEV GEANFNKSKEFVEEVIQRMD VSPDATRISVLQYSYTVTME YAFNGAQSKEEVLRHVREIR YQGGNRTNTGQALQYLSEHS FSPSQGDRVEAPNLVYMVTG NPASDEIKRLPGDIQVVPIG VGPHANMQELERISRPIAPI FIRDFETLPREAPDLVLQTC CS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	519
15N chemical shifts	163
1H chemical shifts	163

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	vWF-A2	1

Entities:

Entity 1, vWF-A2 182 residues - Formula weight is not available

1

GLY

PRO

LEU

GLY

SER

MET

VAL

LEU

ASP

VAL

2

VAL

PHE

VAL

LEU

GLU

GLY

SER

ASP

GLU

VAL

3

GLY

GLU

ALA

ASN

PHE

ASN

LYS

SER

LYS

GLU

4

PHE

VAL

GLU

VAL

ILE

GLN

ARG

MET

ASP

5

VAL

SER

PRO

ASP

ALA

THR

ARG

ILE

SER

VAL

6

LEU

GLN

TYR

SER

TYR

THR

VAL

THR

MET

GLU

7

TYR

ALA

PHE

ASN

GLY

ALA

GLN

SER

LYS

GLU

8

GLU

VAL

LEU

ARG

HIS

VAL

ARG

GLU

ILE

ARG

9

TYR

GLN

GLY

ASN

ARG

THR

ASN

THR

GLY

10

GLN

ALA

LEU

GLN

TYR

LEU

SER

GLU

HIS

SER

11

PHE

SER

PRO

SER

GLN

GLY

ASP

ARG

VAL

GLU

12

ALA

PRO

ASN

LEU

VAL

TYR

MET

VAL

THR

GLY

13

ASN

PRO

ALA

SER

ASP

GLU

ILE

LYS

ARG

LEU

14

PRO

GLY

ASP

ILE

GLN

VAL

PRO

ILE

GLY

15

VAL

GLY

PRO

HIS

ALA

ASN

MET

GLN

GLU

LEU

16

GLU

ARG

ILE

SER

ARG

PRO

ILE

ALA

PRO

ILE

17

PHE

ILE

ARG

ASP

PHE

GLU

THR

LEU

PRO

ARG

18

GLU

ALA

PRO

ASP

LEU

VAL

LEU

GLN

THR

CYS

19

CYS

SER

Samples:

sample_1: vWF-A2, [U-99% 13C; U-99% 15N], 1.3 mM; Tris-HCl buffer 50 mM; calcium chloride 2 mM

sample_conditions_1: pH: 8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCANH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

MAGRO - chemical shift assignment

FLYA - chemical shift assignment

CcpNMR - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 700 MHz

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