BMRB Entry 25109
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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/BMR25109
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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
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 428 |
15N chemical shifts | 116 |
1H chemical shifts | 712 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | MAVS CARD | 1 |
Entities:
Entity 1, MAVS CARD 102 residues - 11817.452 Da.
1 | GLY | SER | MET | PRO | PHE | ALA | GLU | ASP | LYS | THR | ||||
2 | TYR | LYS | TYR | ILE | CYS | ARG | ASN | PHE | SER | ASN | ||||
3 | PHE | CYS | ASN | VAL | ASP | VAL | VAL | GLU | ILE | LEU | ||||
4 | PRO | TYR | LEU | PRO | CYS | LEU | THR | ALA | ARG | ASP | ||||
5 | GLN | ASP | ARG | LEU | ARG | ALA | THR | CYS | THR | LEU | ||||
6 | SER | GLY | ASN | ARG | ASP | THR | LEU | TRP | HIS | LEU | ||||
7 | PHE | ASN | THR | LEU | GLN | ARG | ARG | PRO | GLY | TRP | ||||
8 | VAL | GLU | TYR | PHE | ILE | ALA | ALA | LEU | ARG | GLY | ||||
9 | CYS | GLU | LEU | VAL | ASP | LEU | ALA | ASP | GLU | VAL | ||||
10 | ALA | SER | VAL | TYR | GLN | SER | TYR | GLN | PRO | ARG | ||||
11 | THR | SER |
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:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_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