BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 50020

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50020

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

Title: Structural and biophysical characterization of the type VII collagen vWFA2 subdomain leads to identification of two binding sites and helps understanding the consequences of autoimmunity against type VII collagen   PubMed: 32031736

Deposition date: 2019-09-23 Original release date: 2020-02-13

Authors: Gebauer, Jan; Flachsenberg, Florian; Windler, Cordula; Richer, Barbara; Baumann, Ulrich; Seeger, Karsten

Citation: Gebauer, Jan; Flachsenberg, Florian; Windler, Cordula; Richer, Barbara; Baumann, Ulrich; Seeger, Karsten. "Structural and biophysical characterization of the type VII collagen vWFA2 subdomain leads to identification of two binding sites"  FEBS Open Bio. 10, 580-592 (2020).

Assembly members:
entity_1, polymer, 196 residues, Formula weight is not available

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pTWIN1

Entity Sequences (FASTA):
entity_1: GRAMGACSHGPVDVVFLLHA TRDNAHNAEAVRRVLERLVS ALGPLGPQAAQVGLLTYSHR PSPLFPLNSSHDLGIILRKI RDIPYVDPSGNNLGTAVTTA HRYLLASNAPGRRQQVPGVM VLLVDEPLRGDILSPIREAQ TSGLKVMALSLVGADPEQLR RLAPGTDPIQNFFAVDNGPG LDRAVSDLAVALCQAA

Data sets:
Data typeCount
T1 relaxation values140
T2 relaxation values140
heteronuclear NOE values141
residual dipolar couplings288

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1mvWFA21

Entities:

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

1   GLYARGALAMETGLYALACYSSERHISGLY
2   PROVALASPVALVALPHELEULEUHISALA
3   THRARGASPASNALAHISASNALAGLUALA
4   VALARGARGVALLEUGLUARGLEUVALSER
5   ALALEUGLYPROLEUGLYPROGLNALAALA
6   GLNVALGLYLEULEUTHRTYRSERHISARG
7   PROSERPROLEUPHEPROLEUASNSERSER
8   HISASPLEUGLYILEILELEUARGLYSILE
9   ARGASPILEPROTYRVALASPPROSERGLY
10   ASNASNLEUGLYTHRALAVALTHRTHRALA
11   HISARGTYRLEULEUALASERASNALAPRO
12   GLYARGARGGLNGLNVALPROGLYVALMET
13   VALLEULEUVALASPGLUPROLEUARGGLY
14   ASPILELEUSERPROILEARGGLUALAGLN
15   THRSERGLYLEULYSVALMETALALEUSER
16   LEUVALGLYALAASPPROGLUGLNLEUARG
17   ARGLEUALAPROGLYTHRASPPROILEGLN
18   ASNPHEPHEALAVALASPASNGLYPROGLY
19   LEUASPARGALAVALSERASPLEUALAVAL
20   ALALEUCYSGLNALAALA

Samples:

sample_1: mvWFA2, [U-99% 15N], 1 mM; potassium phosphate 10 mM; H2O 90 % v/v; D2O 10 % v/v

sample_2: mvWFA2, [U-100% 15N], 0.6 mM; sodium phosphate 10 mM; D2O, [U-2H], 10 % v/v; PEG 4.2 % w/v; 1-Hexanol 1.5 % v/v

sample_3: mvWFA2, [U-100% 15N], 0.6 mM; sodium phosphate 10 mM; D2O, [U-2H], 10 % v/v; PEG 4.2 % w/v; 1-Hexanol 1.9 % v/v; CTAB 0.1 % w/v

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
15N-(1H) NOEsample_1isotropicsample_conditions_1
hsqct1etf3gpsi3dsample_1isotropicsample_conditions_1
hsqct2etf3gpsi3dsample_1isotropicsample_conditions_1
hsqcf3gpiaphsiwgsample_2isotropicsample_conditions_1
hsqcf3gpiaphsiwgsample_3isotropicsample_conditions_1
hsqcf3gpiaphsiwgsample_1isotropicsample_conditions_1

Software:

CcpNMR, CCPN - data analysis

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker DRX 500 MHz