BMRB Entry 30874

Name: Structure and Interactions of DED1 of human cFLIP
Published: 2021-11-28

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PDB ID: 7lxc
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30874
MolProbity Validation Chart

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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:

Structure and Interactions of DED1 of human cFLIP

Deposition date:

2021-03-03

Original release date:

2021-11-28

Authors:

Panaitiu, A.; Basiashvili, T.; Mierke, D.; Pellegrini, M.

Citation:

Citation: Panaitiu, A.; Basiashvili, T.; Mierke, D.; Pellegrini, M.. "An engineered construct of cFLIP provides insight into DED1 structure and interactions" Structure 30, 229-239 (2021).
PubMed: 34800372

Assembly members:

Assembly members:
entity_1, polymer, 105 residues, 12425.535 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(DE3) Vector: pET30b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MHHHHHHMSAEVIHQVEEAL SSSELTELKYLCLGRVGKRK LERVQSGVRDLLDILRERGK LSVGDLAELLYRVRRFDLLK RILKMDRKAVETHLLRNPHL VSDYR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	662
15N chemical shifts	189
1H chemical shifts	1388

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_1 105 residues - 12425.535 Da.

1

MET

HIS

MET

SER

ALA

2

GLU

VAL

ILE

HIS

GLN

VAL

GLU

ALA

LEU

3

SER

GLU

LEU

THR

GLU

LEU

LYS

TYR

4

LEU

CYS

LEU

GLY

ARG

VAL

GLY

LYS

ARG

LYS

5

LEU

GLU

ARG

VAL

GLN

SER

GLY

VAL

ARG

ASP

6

LEU

ASP

ILE

LEU

ARG

GLU

ARG

GLY

LYS

7

LEU

SER

VAL

GLY

ASP

LEU

ALA

GLU

LEU

8

TYR

ARG

VAL

ARG

PHE

ASP

LEU

LYS

9

ARG

ILE

LEU

LYS

MET

ASP

ARG

LYS

ALA

VAL

10

GLU

THR

HIS

LEU

ARG

ASN

PRO

HIS

LEU

11

VAL

SER

ASP

TYR

ARG

Samples:

sample_1: entity_1, [U-13C; U-15N], 300 uM; sodium succinate 20 mM; sodium chloride 250 mM; DTT 3 mM; pefabloc 0.2 mM

sample_conditions_1: ionic strength: 0.27 M; pH: 5.8; pressure: 1 atm; temperature: 291 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

CS-ROSETTA, Shen, Vernon, Baker and Bax - structure calculation

TopSpin v3.2, Bruker Biospin - collection

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - peak picking

NMR spectrometers:

Bruker AVANCE 700 MHz

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