BMRB Entry 25750

Name: NMR Structure of the C-terminal Coiled-Coil Domain of CIN85
Published: 2016-07-11

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PDB ID: 2n64
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25750
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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:

NMR Structure of the C-terminal Coiled-Coil Domain of CIN85

Deposition date:

2015-08-11

Original release date:

2016-07-11

Authors:

Habeck, Michael; Becker, Stefan; Griesinger, Christian; Wong, Leo

Citation:

Citation: Kuehn, Julius; Wong, Leo; Pirkuliyeva, Sona; Batista, Facundo; Schwiegk, Claudia; Gencalp, Kevser; Urlaub, Henning; Habeck, Michael; Becker, Stefan; Griesinger, Christian; Wienands, Juergen. "The adaptor protein CIN85 assembles intracellular signaling clusters for B cell activation" Sci. Signal. 9, 66-66 (2016).
PubMed: 27353366

Assembly members:

Assembly members:
CIN85_CC-domain, polymer, 75 residues, 8762.257 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 Vector: pET16b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CIN85_CC-domain: GHMEGKPKMEPAASSQAAVE ELRTQVRELRSIIETMKDQQ KREIKQLLSELDEEKKIRLR LQMEVNDIKKALQSK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list
heteronucl_T2_relaxation
- heteronuclear_T2_list

Data type	Count
13C chemical shifts	277
15N chemical shifts	79
1H chemical shifts	301
T2 relaxation values	60

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CIN85 CC-domain, chain 1	1
2	CIN85 CC-domain, chain 2	1
3	CIN85 CC-domain, chain 3	1

Entities:

Entity 1, CIN85 CC-domain, chain 1 75 residues - 8762.257 Da.

1

GLY

HIS

MET

GLU

GLY

LYS

PRO

LYS

MET

GLU

2

PRO

ALA

SER

GLN

ALA

VAL

GLU

3

GLU

LEU

ARG

THR

GLN

VAL

ARG

GLU

LEU

ARG

4

SER

ILE

GLU

THR

MET

LYS

ASP

GLN

5

LYS

ARG

GLU

ILE

LYS

GLN

LEU

SER

GLU

6

LEU

ASP

GLU

LYS

ILE

ARG

LEU

ARG

7

LEU

GLN

MET

GLU

VAL

ASN

ASP

ILE

LYS

8

ALA

LEU

GLN

SER

LYS

Samples:

sample_1: CIN85 CC-domain, [U-13C; U-15N; U-2H], 2 mM

sample_2: CIN85 CC-domain, [U-13C; U-15N; U-2H], 2 mM; CIN85 CC-domain, [U-2H], 2 mM

sample_conditions: pH: 6.9; pressure: 1 atm; temperature: 305 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY-HSQC	sample_1	isotropic	sample_conditions
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions
3D HNCACB	sample_1	isotropic	sample_conditions
3D HNCO	sample_1	isotropic	sample_conditions
3D HN(CA)CO	sample_1	isotropic	sample_conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions
2D TRACT	sample_1	isotropic	sample_conditions

Software:

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 800 MHz

UNP	Q96B97
AlphaFold	Q9NYR0