BMRB Entry 34294

Name: Solution structure of rat RIP2 caspase recruitment domain
Published: 2018-10-29

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PDB ID: 6gwm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34294
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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:

Solution structure of rat RIP2 caspase recruitment domain

Deposition date:

2018-06-25

Original release date:

2018-10-29

Authors:

Mineev, K.; Goncharuk, S.; Artemieva, L.; Arseniev, A.

Citation:

Citation: Goncharuk, S.; Artemieva, L.; Tabakmakher, V.; Arseniev, A.; Mineev, K.. "CARD domain of rat RIP2 kinase: Refolding, solution structure, pH-dependent behavior and protein-protein interactions." PLoS ONE 13, e0206244-e0206244 (2018).
PubMed: 30352081

Assembly members:

Assembly members:
entity_1, polymer, 125 residues, 14075.079 Da.

Natural source:

Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MHHHHHHGSGSGLVPRGSGI AQQWIQSKREAIVSQMTEAC LNQSLDALLSRDLIMKEDYE LISTKPTRTAKVRQLLDTSD IQGEEFARVIVQKLKDNKQM GLQPYPEVLLVSRTPSSNVL QNKTL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	530
15N chemical shifts	131
1H chemical shifts	881

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 125 residues - 14075.079 Da.

1

MET

HIS

GLY

SER

GLY

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

GLY

ILE

3

ALA

GLN

TRP

ILE

GLN

SER

LYS

ARG

GLU

4

ALA

ILE

VAL

SER

GLN

MET

THR

GLU

ALA

CYS

5

LEU

ASN

GLN

SER

LEU

ASP

ALA

LEU

SER

6

ARG

ASP

LEU

ILE

MET

LYS

GLU

ASP

TYR

GLU

7

LEU

ILE

SER

THR

LYS

PRO

THR

ARG

THR

ALA

8

LYS

VAL

ARG

GLN

LEU

ASP

THR

SER

ASP

9

ILE

GLN

GLY

GLU

PHE

ALA

ARG

VAL

ILE

10

VAL

GLN

LYS

LEU

LYS

ASP

ASN

LYS

GLN

MET

11

GLY

LEU

GLN

PRO

TYR

PRO

GLU

VAL

LEU

12

VAL

SER

ARG

THR

PRO

SER

ASN

VAL

LEU

13

GLN

ASN

LYS

THR

LEU

Samples:

sample_1: CARD domain of rat RIP2, [U-99% 13C; U-99% 15N], 0.5 ± 0.05 mM; TCEP 1 mM; sodium azide 0.001%

sample_conditions_1: ionic strength: 0 mM; pH: 4.2; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1

Software:

CYANA v3.97, Guntert P. - structure calculation

CARA v1.9.4, Keller and Wuthrich - chemical shift assignment

TOPSPIN v3.2, Bruker Biospin - processing

NMR spectrometers:

Bruker AvanceIII 800 MHz

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