BMRB Entry 17549

Name: Backbone Resonance Assignment of the von-Willebrand-factor-A-like domain 2 of type VII collagen
Published: 2011-05-04

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17549

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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:

Backbone Resonance Assignment of the von-Willebrand-factor-A-like domain 2 of type VII collagen

Deposition date:

2011-03-24

Original release date:

2011-05-04

Authors:

Leineweber, Sarah

Citation:

Citation: Leineweber, Sarah; Schonig, Sarah; Seeger, Karsten. "Insight into interactions of the von-Willebrand-factor-A-like domain 2 with the FNIII-like domain 9 of collagen VII by NMR and SPR." FEBS Lett. 585, 1748-1752 (2011).
PubMed: 21570975

Assembly members:

Assembly members:
mvWFA2, polymer, 196 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: pTWIN1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
mvWFA2: GRAMGACSHGPVDVVFLLHA TRDNAHNAEAVRRVLERLVS ALGPLGPQAAQVGLLTYSHR PSPLFPLNSSHDLGIILRKI RDIPYVDPSGNNLGTAVTTA HRYLLASNAPGRRQQVPGVM VLLVDEPLRGDILSPIREAQ TSGLKVMALSLVGADPEQLR RLAPGTDPIQNFFAVDNGPG LDRAVSDLAVALCQAA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	325
15N chemical shifts	167
1H chemical shifts	366

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	mvWFA2	1

Entities:

Entity 1, mvWFA2 196 residues - Formula weight is not available

1

GLY

ARG

ALA

MET

GLY

ALA

CYS

SER

HIS

GLY

2

PRO

VAL

ASP

VAL

PHE

LEU

HIS

ALA

3

THR

ARG

ASP

ASN

ALA

HIS

ASN

ALA

GLU

ALA

4

VAL

ARG

VAL

LEU

GLU

ARG

LEU

VAL

SER

5

ALA

LEU

GLY

PRO

LEU

GLY

PRO

GLN

ALA

6

GLN

VAL

GLY

LEU

THR

TYR

SER

HIS

ARG

7

PRO

SER

PRO

LEU

PHE

PRO

LEU

ASN

SER

8

HIS

ASP

LEU

GLY

ILE

LEU

ARG

LYS

ILE

9

ARG

ASP

ILE

PRO

TYR

VAL

ASP

PRO

SER

GLY

10

ASN

LEU

GLY

THR

ALA

VAL

THR

ALA

11

HIS

ARG

TYR

LEU

ALA

SER

ASN

ALA

PRO

12

GLY

ARG

GLN

VAL

PRO

GLY

VAL

MET

13

VAL

LEU

VAL

ASP

GLU

PRO

LEU

ARG

GLY

14

ASP

ILE

LEU

SER

PRO

ILE

ARG

GLU

ALA

GLN

15

THR

SER

GLY

LEU

LYS

VAL

MET

ALA

LEU

SER

16

LEU

VAL

GLY

ALA

ASP

PRO

GLU

GLN

LEU

ARG

17

ARG

LEU

ALA

PRO

GLY

THR

ASP

PRO

ILE

GLN

18

ASN

PHE

ALA

VAL

ASP

ASN

GLY

PRO

GLY

19

LEU

ASP

ARG

ALA

VAL

SER

ASP

LEU

ALA

VAL

20

ALA

LEU

CYS

GLN

ALA

Samples:

sample_1: mvWFA2, [U-100% 13C; U-100% 15N], 2 mM; potassium phosphate 10 mM; TSP 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

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