BMRB Entry 52081

Name: CIN85(163-333)
Published: 2023-12-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52081

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

CIN85(163-333)

Deposition date:

2023-08-15

Original release date:

2023-12-19

Authors:

Sieme, Daniel; Griesinger, Christian

Citation:

Citation: Sieme, Daniel; Engelke, Michael; Rezaei-Ghaleh, Nasrollah; Becker, Stefan; Wienands, Jurgen; Griesinger, Christian. "Autoinhibition in the Signal Transducer CIN85 Modulates B Cell Activation" J. Am. Chem. Soc. 146, 399-409 (2024).
PubMed: 38111344

Assembly members:

Assembly members:
entity_1, polymer, 173 residues, 18889.07 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX4-T

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSGISQDEQLSKSSLRETTG SESDGGDSSSTKSEGANGTV ATAAIQPKKVKGVGFGDIFK DKPIKLRPRSIEVENDFLPV EKTIGKKLPATTATPDSSKT EMDSRTKSKDYCKVIFPYEA QNDDELTIKEGDIVTLINKD CIDVGWWEGELNGRRGVFPD NFVKLLPPDFEKE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	445
15N chemical shifts	170
1H chemical shifts	638

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CIN85(163-333)	1

Entities:

Entity 1, CIN85(163-333) 173 residues - 18889.07 Da.

The first two amino acids (161 and 162) remain after cleaving the purification tag and do not appear in the original protein sequence.

1

GLY

SER

GLY

ILE

SER

GLN

ASP

GLU

GLN

LEU

2

SER

LYS

SER

LEU

ARG

GLU

THR

GLY

3

SER

GLU

SER

ASP

GLY

ASP

SER

4

THR

LYS

SER

GLU

GLY

ALA

ASN

GLY

THR

VAL

5

ALA

THR

ALA

ILE

GLN

PRO

LYS

VAL

6

LYS

GLY

VAL

GLY

PHE

GLY

ASP

ILE

PHE

LYS

7

ASP

LYS

PRO

ILE

LYS

LEU

ARG

PRO

ARG

SER

8

ILE

GLU

VAL

GLU

ASN

ASP

PHE

LEU

PRO

VAL

9

GLU

LYS

THR

ILE

GLY

LYS

LEU

PRO

ALA

10

THR

ALA

THR

PRO

ASP

SER

LYS

THR

11

GLU

MET

ASP

SER

ARG

THR

LYS

SER

LYS

ASP

12

TYR

CYS

LYS

VAL

ILE

PHE

PRO

TYR

GLU

ALA

13

GLN

ASN

ASP

GLU

LEU

THR

ILE

LYS

GLU

14

GLY

ASP

ILE

VAL

THR

LEU

ILE

ASN

LYS

ASP

15

CYS

ILE

ASP

VAL

GLY

TRP

GLU

GLY

GLU

16

LEU

ASN

GLY

ARG

GLY

VAL

PHE

PRO

ASP

17

ASN

PHE

VAL

LYS

LEU

PRO

ASP

PHE

18

GLU

LYS

GLU

Samples:

sample_1: MES 20 mM; sodium chloride 100 mM; CIN85 monomer, [U-13C; U-15N], 1 mM; DSS 0.5 mM; EDTA 0.5 mM; sodium azide 0.01 % w/v; TCEP 1 mM; D2O 5 % v/v

sample_conditions_1: ionic strength: 0.1 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D (HACA)N(CA)CON	sample_1	isotropic	sample_conditions_1
3D (H)CCCON	sample_1	isotropic	sample_conditions_1
3D H(CC)CON	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
2D (HACA)CON	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1

Software:

POKY - chemical shift assignment

NMRPipe - processing

CYANA - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III HD 700 MHz
Bruker AVANCE III HD 900 MHz
Bruker AVANCE NEO 800 MHz