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 25109

Title: Solution NMR structure of MAVS CARD

Deposition date: 2014-07-25 Original release date: 2015-08-31

Authors: Spehr, Johannes; He, Lichun; Luehrs, Thorsten; Ritter, Christiane

Citation: He, Lichun; Bardiaux, Benjamin; Spehr, Johannes; Luehrs, Thorsten; Ritter, Christiane. "High-resolution solid-state NMR structure of the helical signal transduction filament MAVS CARD"  Not known ., .-..

Assembly members:
MAVS_CARD, polymer, 102 residues, 11817.452 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):
MAVS_CARD: GSMPFAEDKTYKYICRNFSN FCNVDVVEILPYLPCLTARD QDRLRATCTLSGNRDTLWHL FNTLQRRPGWVEYFIAALRG CELVDLADEVASVYQSYQPR TS

Data sets:
Data typeCount
13C chemical shifts428
15N chemical shifts116
1H chemical shifts712

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MAVS CARD1

Entities:

Entity 1, MAVS CARD 102 residues - 11817.452 Da.

1   GLYSERMETPROPHEALAGLUASPLYSTHR
2   TYRLYSTYRILECYSARGASNPHESERASN
3   PHECYSASNVALASPVALVALGLUILELEU
4   PROTYRLEUPROCYSLEUTHRALAARGASP
5   GLNASPARGLEUARGALATHRCYSTHRLEU
6   SERGLYASNARGASPTHRLEUTRPHISLEU
7   PHEASNTHRLEUGLNARGARGPROGLYTRP
8   VALGLUTYRPHEILEALAALALEUARGGLY
9   CYSGLULEUVALASPLEUALAASPGLUVAL
10   ALASERVALTYRGLNSERTYRGLNPROARG
11   THRSER

Samples:

sample_1: MAVS CARD, [U-99% 13C; U-99% 15N], 300 uM; sodium phosphate buffer 50 mM; DTT 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 3; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis

PROSA, Guntert - processing

TOPSPIN, Bruker Biospin - collection, processing

UNIO_10 v2.0.2, Thorsten Herrmann - structure calculation

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

ATNOS, Herrmann, Guntert and Wuthrich - structure solution

CANDID v2.0, Herrmann, Guntert and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 25076
PDB
DBJ BAA86585 BAB14684 BAC77356 BAC85473 BAE79738
GB AAH44952 AAZ80417 ABA19229 ABA54890 ABR24162
REF NP_065797 XP_003821366 XP_008973040 XP_008973041 XP_009435017
SP Q7Z434

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