BMRB Entry 19764

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19764
MolProbity Validation Chart

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

Title:
Spatial structure of the dimeric transmembrane domain of Toll-like receptor 3
Deposition date:
2014-02-04
Original release date:
2014-09-15
Authors:
Mineev, Konstantin; Goncharuk, Sergey; Arseniev, Alexander
Citation:

Citation: Mineev, Konstantin; Goncharuk, Sergey; Arseniev, Alexander. "Toll-like Receptor 3 Transmembrane Domain is Able to Perform Various Homotypic Interactions: an NMR Structural Study."  To be Published ., .-..

Assembly members:

Assembly members:
entity, polymer, 34 residues, 4089.984 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: E. coli - cell free   Vector: PET22B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MDSAPFELFFMINTSILLIF IFIVLLIHFEGWRI

Data sets:
Data typeCount
13C chemical shifts168
15N chemical shifts34
1H chemical shifts284

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21

Entities:

Entity 1, entity_1 34 residues - 4089.984 Da.

fragment corresponds to the transmembrane domain of the human TLR3 receptor residues D698-I730

1   METASPSERALAPROPHEGLULEUPHEPHE
2   METILEASNTHRSERILELEULEUILEPHE
3   ILEPHEILEVALLEULEUILEHISPHEGLU
4   GLYTRPARGILE

Samples:

sample_1: entity 0.8 mM; entity, [U-98% 13C; U-98% 15N], 1.2 mM; potassium phosphate 20 mM; sodium azide 1 mM; DPC, [U-99% 2H], 200 mM; H2O 95; D2O 5%

sample_conditions_1: ionic strength: 20 mM; pH: 7.5; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
13C/15N-filtered NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.0, Bruker Biospin - collection

CARA v1.8.5, Keller and Wuthrich - chemical shift assignment, data analysis

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS v+, Cornilescu, Delaglio and Bax - data analysis

qMDD v2.1, Orekhov, Mayzel - processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UNP O15455
PDB
DBJ BAG36884 BAG55028 BAG55029 BAG55030 BAG55031
GB AAC34134 AAH59372 AAH94737 AAH96333 AAH96334
REF NP_001123942 NP_001266163 NP_001266681 NP_001277098 NP_003256
SP O15455
AlphaFold Q504W0 O15455

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