BMRB Entry 16103
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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/BMR16103
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Title: 1H, 13C, and 15N chemical shift assignments for murine FAIM-CTD PubMed: 19168072
Deposition date: 2009-01-01 Original release date: 2009-04-22
Authors: Hemond, Michael; Wagner, Gerhard
Citation: Hemond, Michael; Rothstein, Thomas; Wagner, Gerhard. "Fas Apoptosis Inhibitory Molecule contains a novel beta sandwich in contact with a partially ordered domain" J. Mol. Biol. 386, 1024-1037 (2009).
Assembly members:
FAIM-CTD, polymer, 94 residues, Formula weight is not available
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
FAIM-CTD: GPLGSENRSKTTSTWVLRLD
GEDLRVVLEKDTMDVWCNGQ
KMETAGEFVDDGTETHFSVG
NHDCYIKAVSSGKRKEGIIH
TLIVDNREIPELTQ
- assigned_chemical_shifts
- RDCs
| Data type | Count |
| 13C chemical shifts | 364 |
| 15N chemical shifts | 96 |
| 1H chemical shifts | 561 |
| residual dipolar couplings | 67 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FAIM-CTD monomer | 1 |
Entities:
Entity 1, FAIM-CTD monomer 94 residues - Formula weight is not available
Residues 1-5 are derived from a non-native protease site and polypeptide linker
| 1 | GLY | PRO | LEU | GLY | SER | GLU | ASN | ARG | SER | LYS | ||||
| 2 | THR | THR | SER | THR | TRP | VAL | LEU | ARG | LEU | ASP | ||||
| 3 | GLY | GLU | ASP | LEU | ARG | VAL | VAL | LEU | GLU | LYS | ||||
| 4 | ASP | THR | MET | ASP | VAL | TRP | CYS | ASN | GLY | GLN | ||||
| 5 | LYS | MET | GLU | THR | ALA | GLY | GLU | PHE | VAL | ASP | ||||
| 6 | ASP | GLY | THR | GLU | THR | HIS | PHE | SER | VAL | GLY | ||||
| 7 | ASN | HIS | ASP | CYS | TYR | ILE | LYS | ALA | VAL | SER | ||||
| 8 | SER | GLY | LYS | ARG | LYS | GLU | GLY | ILE | ILE | HIS | ||||
| 9 | THR | LEU | ILE | VAL | ASP | ASN | ARG | GLU | ILE | PRO | ||||
| 10 | GLU | LEU | THR | GLN |
Samples:
sample_1: FAIM-CTD, [U-99% 13C; U-99% 15N], 0.25 – 0.5 mM; sodium chloride 10 mM; TRIS 10 mM; DTT 5 mM
sample_2: FAIM-CTD, [U-99% 13C; U-99% 15N], 0.25 mM; sodium chloride 10 mM; TRIS 10 mM; DTT 5 mM; Pf1 filamentous phage 0.6% w/v
sample_3: FAIM-CTD, [U-99% 13C], 1.8 mM; sodium chloride 10 mM; TRIS 10 mM; DTT 5 mM
sample_4: FAIM-CTD, [U-10% 13C], 0.5 mM; sodium chloride 10 mM; TRIS 10 mM; DTT 5 mM
sample_5: FAIM-CTD, [U-99% 15N], 0.25 – 0.9 mM; sodium chloride 10 mM; TRIS 10 mM; DTT 5 mM
sample_6: FAIM-CTD 1.4 mM; sodium chloride 10 mM; TRIS 10 mM; DTT 5 mM
sample_conditions_1: ionic strength: 10 mM; pH: 7.3; pressure: 1.0 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | anisotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_5 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_5 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_6 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D CCH-COSY | sample_3 | isotropic | sample_conditions_1 |
Software:
NMRPipe v2.4 Rev 2006.095.11.35, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY v3.110, Goddard - data analysis
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Varian INOVA 500 MHz
- Bruker Avance 900 MHz
Related Database Links:
| PDB | |
| DBJ | BAB24225 |
| GB | AAD23879 AAH79662 EDL20994 EDL20995 |
| REF | NP_001116323 NP_035940 |
| SP | Q9WUD8 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts