BMRB Entry 34648

Name: NMR solution structure of the C6 domain of von Willebrand Factor
Published: 2022-07-21

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PDB ID: 7p4n
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34648
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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:

NMR solution structure of the C6 domain of von Willebrand Factor

Deposition date:

2021-07-12

Original release date:

2022-07-21

Authors:

Hennig, J.; Chen, P.-C.; Simon, B.

Citation:

Citation: Chen, Po-Chia; Kutzki, Fabian; Mojzisch, Angelika; Simon, Bernd; Xu, Emma-Ruoqi; Aponte-Santamaria, Camilo; Horny, Kai; Jeffries, Cy; Schneppenheim, Reinhard; Wilmanns, Matthias; Brehm, Maria; Grater, Frauke; Hennig, Janosch. "Structure and dynamics of the von Willebrand Factor C6 domain" J. Struct. Biol. 214, 107923-107923 (2022).
PubMed: 36410652

Assembly members:

Assembly members:
entity_1, polymer, 78 residues, 8703.000 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 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSMATACTIQLRGGQIMTLK RDETLQDGCDTHFCKVNERG EYFWEKRVTGCPPFDEHKCL AEGGKIMKIPGTCCDTCE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	307
15N chemical shifts	72
1H chemical shifts	480

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 78 residues - 8703.000 Da.

1

GLY

SER

MET

ALA

THR

ALA

CYS

THR

ILE

GLN

2

LEU

ARG

GLY

GLN

ILE

MET

THR

LEU

LYS

3

ARG

ASP

GLU

THR

LEU

GLN

ASP

GLY

CYS

ASP

4

THR

HIS

PHE

CYS

LYS

VAL

ASN

GLU

ARG

GLY

5

GLU

TYR

PHE

TRP

GLU

LYS

ARG

VAL

THR

GLY

6

CYS

PRO

PHE

ASP

GLU

HIS

LYS

CYS

LEU

7

ALA

GLU

GLY

LYS

ILE

MET

LYS

ILE

PRO

8

GLY

THR

CYS

ASP

THR

CYS

GLU

Samples:

sample_1: von Willebrand Factor C6 domain, [U-13C; U-15N], 300 uM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1.013 bar; 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
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

ARIA, Linge, O'Donoghue and Nilges - structure calculation

NMR spectrometers:

Bruker AVANCE III 600 MHz

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