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Biological Magnetic Resonance Data Bank


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BMRB Entry 19687

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19687
MolProbity Validation Chart

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Title: immune signalling subunit

Deposition date: 2013-12-15 Original release date: 2014-02-10

Authors: Headey, Stephen; Berry, Richard; Rossjohn, Jamie

Citation: Berry, Richard; Headey, Stephen; Call, Matthew; McCluskey, James; Tregaskes, Clive; Kaufman, Jim; Koh, Ruide; Mohanty, Biswaranjan; Scanlon, Martin; Call, Melissa; Rossjohn, Jamie. "immune signalling subunit"  Not known ., .-..

Assembly members:
entity, polymer, 178 residues, 19569.904 Da.

Natural source:   Common Name: chicken   Taxonomy ID: 9031   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Gallus gallus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity: GSHMGQEEFAVEISGTTVTI TCPSSGDDIKWKPDPALGDN NKYIIQNHDSSPLTVSCTAG DQEHTMYLNAKVGSADDAKK DAAKKDDAKKDDAKKDGSVA KLGVHGLSMSVKEVSGKVFL QCQESKDLNTNYLWKKGKEE LGNMRQLDLGAIYDDPRGTY TCQRDENVNSTLHVHYRM

Data sets:
Data typeCount
1H chemical shifts829
13C chemical shifts408
15N chemical shifts144

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1immune signalling subunit1

Entities:

Entity 1, immune signalling subunit 178 residues - 19569.904 Da.

1   GLYSERHISMETGLYGLNGLUGLUPHEALA
2   VALGLUILESERGLYTHRTHRVALTHRILE
3   THRCYSPROSERSERGLYASPASPILELYS
4   TRPLYSPROASPPROALALEUGLYASPASN
5   ASNLYSTYRILEILEGLNASNHISASPSER
6   SERPROLEUTHRVALSERCYSTHRALAGLY
7   ASPGLNGLUHISTHRMETTYRLEUASNALA
8   LYSVALGLYSERALAASPASPALALYSLYS
9   ASPALAALALYSLYSASPASPALALYSLYS
10   ASPASPALALYSLYSASPGLYSERVALALA
11   LYSLEUGLYVALHISGLYLEUSERMETSER
12   VALLYSGLUVALSERGLYLYSVALPHELEU
13   GLNCYSGLNGLUSERLYSASPLEUASNTHR
14   ASNTYRLEUTRPLYSLYSGLYLYSGLUGLU
15   LEUGLYASNMETARGGLNLEUASPLEUGLY
16   ALAILETYRASPASPPROARGGLYTHRTYR
17   THRCYSGLNARGASPGLUASNVALASNSER
18   THRLEUHISVALHISTYRARGMET

Samples:

sample_1: protein, [U-98% 13C; U-98% 15N], 0.5 mM; HEPES 50 mM; arginine 125 mM; glutamate 125 mM; azide 0.01%; Roche protease inhibitor 0.01%; EDTA 0.5 mM

deuterated: protein, [U-100% 13C; U-100% 15N; U-80% 2H], 0.5 mM; HEPES 50 mM; arginine 125 mM; glutamate 125 mM; azide 0.01%; Roche protease inhibitor 0.01%; EDTA 0.5 mM

sample_conditions_1: temperature: 293 K; pH: 7.6; pressure: 1 atm; ionic strength: 0.3 M

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HN(COCA)CBdeuteratedisotropicsample_conditions_1
3D HNCACBdeuteratedisotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAdeuteratedisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

XEASY, Bartels et al. - data analysis

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
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