BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 26061

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR26061
MolProbity Validation Chart

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Title: NMR solution structure of MAL/TIRAP TIR domain   PubMed: 28739909

Deposition date: 2016-05-27 Original release date: 2017-05-30

Authors: Lavrencic, Peter; Mobli, Mehdi

Citation: Hughes, Mark; Lavrencic, Peter; Coll, Rebecca; Ve, Thomas; Ryan, Dylan; Williams, Niamh; Menon, Deepthi; Mansell, Ashley; Board, Philip; Mobli, Mehdi; Kobe, Bostjan; O'Neill, Luke. "Solution structure of the TLR adaptor MAL/TIRAP reveals an intact BB loop and supports MAL Cys91 glutathionylation for signaling"  Proc. Natl. Acad. Sci. U.S.A. 114, E6480-E6489 (2017).

Assembly members:
entity, polymer, 143 residues, 15726.982 Da.

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
entity: SSRWSKDYDVCVCHSEEDLV AAQDLVSYLEGSTASLRAFL QLRDATPGGAIVSELCQALS SSHCRVLLITPGFLQDPWCK YQMLQALTEAPGAEGCTIPL LSGLSRAAYPPELRFMYYVD GRGPDGGFRQVKEAVMRYLQ TLS

Data sets:
Data typeCount
13C chemical shifts419
15N chemical shifts104
1H chemical shifts662

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 143 residues - 15726.982 Da.

1   SERSERARGTRPSERLYSASPTYRASPVAL
2   CYSVALCYSHISSERGLUGLUASPLEUVAL
3   ALAALAGLNASPLEUVALSERTYRLEUGLU
4   GLYSERTHRALASERLEUARGALAPHELEU
5   GLNLEUARGASPALATHRPROGLYGLYALA
6   ILEVALSERGLULEUCYSGLNALALEUSER
7   SERSERHISCYSARGVALLEULEUILETHR
8   PROGLYPHELEUGLNASPPROTRPCYSLYS
9   TYRGLNMETLEUGLNALALEUTHRGLUALA
10   PROGLYALAGLUGLYCYSTHRILEPROLEU
11   LEUSERGLYLEUSERARGALAALATYRPRO
12   PROGLULEUARGPHEMETTYRTYRVALASP
13   GLYARGGLYPROASPGLYGLYPHEARGGLN
14   VALLYSGLUALAVALMETARGTYRLEUGLN
15   THRLEUSER

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 300 uM; TRIS 20 mM; D2O 5%; sodium chloride 200 mM; H2O 95%

sample_conditions_1: ionic strength: 0.2 M; pH: 8.6; pressure: 1 atm; temperature: 291 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

TALOS vTALOS+, Cornilescu, Delaglio and Bax - chemical shift calculation

CCPNMR v2.4, CCPN - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - processing

Rowland_NMR_toolkit v3, JC Hoch et al. - processing

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 900 MHz

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