BMRB Entry 17237

Name: NMR Structure of hFn14
Published: 2013-06-04

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PDB ID: 2kmz
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17237
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR Structure of hFn14

Deposition date:

2010-10-05

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:
Fn14, polymer, 53 residues, 5615.414 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: Pichia Pastoris Vector: N/A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Fn14: EQAPGTAPCSRGSSWSADLD KCMDCASCRARPHSDFCLGC AAAPPAPFRLLWP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	33
1H chemical shifts	180

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hFn14	1

Entities:

Entity 1, hFn14 53 residues - 5615.414 Da.

Extracellular Cys-rich domain of human Fn14, the recombinant protein contained a C-terminal Myc-His tag.

1

GLU

GLN

ALA

PRO

GLY

THR

ALA

PRO

CYS

SER

2

ARG

GLY

SER

TRP

SER

ALA

ASP

LEU

ASP

3

LYS

CYS

MET

ASP

CYS

ALA

SER

CYS

ARG

ALA

4

ARG

PRO

HIS

SER

ASP

PHE

CYS

LEU

GLY

CYS

5

ALA

PRO

ALA

PRO

PHE

ARG

LEU

6

LEU

TRP

PRO

Samples:

sample: hFn14, [U-99% 15N], 700 uM; sodium phosphate 10 mM; sodium chloride 137 mM; potassium chloride 2.7 mM; H2O 95%; D2O 5%

sample_2: hFn14 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
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1

Software:

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

SPARKY v3.11, Goddard - data analysis

NMR spectrometers:

Bruker Avance 600 MHz MHz

BMRB	11346
PDB	2EQP 2KMZ 2RPJ
DBJ	BAA94792 BAJ20302
GB	AAF69108 AAH02718 ABM83894 ABM87215 EAW85429
REF	NP_057723 XP_001089176 XP_001165479 XP_002826080 XP_003269240
SP	Q9NP84
AlphaFold	Q9NP84