BMRB Entry 17247

Name: Solution NMR Structure of xenopus Fn14
Published: 2013-06-04

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PDB ID: 2kn0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17247
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR Structure of xenopus Fn14

Deposition date:

2010-10-11

Original release date:

2013-06-04

Authors:

Pellegrini, M.; Willen, L.; Perroud, M.; Krushinskie, D.; Strauch, K.; Cuervo, H.; Sun, Y.; Day, E.; Schneider, P.; Zheng, T.

Citation:

Citation: Pellegrini, Maria; Willen, Laure; Perroud, Mai; Krushinskie, Dennis; Strauch, Kathy; Cuervo, Hernan; Day, Eric; Schneider, Pascal; Zheng, Timothy. "Structure of the extracellular domains of human and Xenopus Fn14: implications in the evolution of TWEAK and Fn14 interactions." FEBS J. 280, 1818-1829 (2013).
PubMed: 23438059

Assembly members:

Assembly members:
xeFn14, polymer, 66 residues, 5682.339 Da.

Natural source:

Natural source: Common Name: African clawed frog Taxonomy ID: 8355 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Xenopus laevis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Pichia Pastoris Vector: N/A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
xeFn14: SQGECPEGRAYSQDLGKCME CSVCKNSEKSDFCQNCPSKT EQPDFPWIWVEQKLISEEDL HHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	36
1H chemical shifts	211

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	xeFn14	1

Entities:

Entity 1, xeFn14 66 residues - 5682.339 Da.

the recombinant protein fragment contained a C-terminal Myc-His tag, the tag residues were not included in the structure calculations

1

SER

GLN

GLY

GLU

CYS

PRO

GLU

GLY

ARG

ALA

2

TYR

SER

GLN

ASP

LEU

GLY

LYS

CYS

MET

GLU

3

CYS

SER

VAL

CYS

LYS

ASN

SER

GLU

LYS

SER

4

ASP

PHE

CYS

GLN

ASN

CYS

PRO

SER

LYS

THR

5

GLU

GLN

PRO

ASP

PHE

PRO

TRP

ILE

TRP

VAL

6

GLU

GLN

LYS

LEU

ILE

SER

GLU

ASP

LEU

7

HIS

Samples:

sample: xeFn14, [U-99% 15N], 500 – 700 uM; sodium phosphate 10 mM; sodium chloride 137 mM; potassium chloride 2.7 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 140 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample	isotropic	sample_conditions_1

Software:

CNS v1.1, Brunger A. T. et.al. - structure solution

SPARKY v3.11, Goddard - data analysis

NMR spectrometers:

Bruker Avance 600 MHz

PDB	2KN0
GB	AAI69735 AAI69737 AAR21225
REF	NP_001083640