BMRB Entry 52081

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

Data sets:
Data typeCount
13C chemical shifts445
15N chemical shifts170
1H chemical shifts638

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1CIN85(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   GLYSERGLYILESERGLNASPGLUGLNLEU
2   SERLYSSERSERLEUARGGLUTHRTHRGLY
3   SERGLUSERASPGLYGLYASPSERSERSER
4   THRLYSSERGLUGLYALAASNGLYTHRVAL
5   ALATHRALAALAILEGLNPROLYSLYSVAL
6   LYSGLYVALGLYPHEGLYASPILEPHELYS
7   ASPLYSPROILELYSLEUARGPROARGSER
8   ILEGLUVALGLUASNASPPHELEUPROVAL
9   GLULYSTHRILEGLYLYSLYSLEUPROALA
10   THRTHRALATHRPROASPSERSERLYSTHR
11   GLUMETASPSERARGTHRLYSSERLYSASP
12   TYRCYSLYSVALILEPHEPROTYRGLUALA
13   GLNASNASPASPGLULEUTHRILELYSGLU
14   GLYASPILEVALTHRLEUILEASNLYSASP
15   CYSILEASPVALGLYTRPTRPGLUGLYGLU
16   LEUASNGLYARGARGGLYVALPHEPROASP
17   ASNPHEVALLYSLEULEUPROPROASPPHE
18   GLULYSGLU

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:

NameSampleSample stateSample conditions
3D (HACA)N(CA)CONsample_1isotropicsample_conditions_1
3D (H)CCCONsample_1isotropicsample_conditions_1
3D H(CC)CONsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D (HACA)CONsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_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

Related Database Links:

UNP Q96B97

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