BMRB Entry 27285
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27285
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Mallis, Robert; Arthanari, Haribabu; Lang, Matt; Reinherz, Ellis; Wagner, Gerhard. "NMR-Directed Design of PreTCRbeta and pMHC Molecules Implies a Distinct Geometry for preTCR Relative to alphabetaTCR Recognition of pMHC" J. Biol. Chem. 293, 754-766 (2018).
PubMed: 29101227
Assembly members:
H-2Kb, polymer, 281 residues, 32348.20 Da.
VSV8, polymer, 8 residues, Formula weight is not available
b2m, polymer, 99 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 Vector: pet11d
Entity Sequences (FASTA):
H-2Kb: MGPHSLRYFVTAVSRPGLGE
PRYMEVGYVDDTEFVRFDSD
AENPRYEPRARWMEQEGPEY
WERETQKAKGNEQSFRVDLR
TLLGYYNQSKGGSHTIQVIS
GCEVGSDGRLLRGYQQYAYD
GCDYIALNEDLKTWTAADMA
ALITKHKWEQAGEAERLRAY
LEGTCVEWLRRYLKNGNATL
LRTDSPKAHVTHHSRPEDKV
TLRCWALGFYPADITLTWQL
NGEELIQDMELVETRPAGDG
TFQKWASVVVPLGKEQYYTC
HVYHQGLPEPLTLRWEPPPS
T
VSV8: RGYVYQGL
b2m: IQKTPQIQVYSRHPPENGKP
NILNCYVTQFHPPHIEIQML
KNGKKIPKVEMSDMSFSKDW
SFYILAHTEFTPTETDTYAC
RVKHDSMAEPKTVYWDRDM
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 296 |
| 15N chemical shifts | 196 |
| 1H chemical shifts | 196 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | H-2Kb | 1 |
| 2 | VSV8 | 2 |
| 3 | b2m | 3 |
Entities:
Entity 1, H-2Kb 281 residues - 32348.20 Da.
| 1 | MET | GLY | PRO | HIS | SER | LEU | ARG | TYR | PHE | VAL | ||||
| 2 | THR | ALA | VAL | SER | ARG | PRO | GLY | LEU | GLY | GLU | ||||
| 3 | PRO | ARG | TYR | MET | GLU | VAL | GLY | TYR | VAL | ASP | ||||
| 4 | ASP | THR | GLU | PHE | VAL | ARG | PHE | ASP | SER | ASP | ||||
| 5 | ALA | GLU | ASN | PRO | ARG | TYR | GLU | PRO | ARG | ALA | ||||
| 6 | ARG | TRP | MET | GLU | GLN | GLU | GLY | PRO | GLU | TYR | ||||
| 7 | TRP | GLU | ARG | GLU | THR | GLN | LYS | ALA | LYS | GLY | ||||
| 8 | ASN | GLU | GLN | SER | PHE | ARG | VAL | ASP | LEU | ARG | ||||
| 9 | THR | LEU | LEU | GLY | TYR | TYR | ASN | GLN | SER | LYS | ||||
| 10 | GLY | GLY | SER | HIS | THR | ILE | GLN | VAL | ILE | SER | ||||
| 11 | GLY | CYS | GLU | VAL | GLY | SER | ASP | GLY | ARG | LEU | ||||
| 12 | LEU | ARG | GLY | TYR | GLN | GLN | TYR | ALA | TYR | ASP | ||||
| 13 | GLY | CYS | ASP | TYR | ILE | ALA | LEU | ASN | GLU | ASP | ||||
| 14 | LEU | LYS | THR | TRP | THR | ALA | ALA | ASP | MET | ALA | ||||
| 15 | ALA | LEU | ILE | THR | LYS | HIS | LYS | TRP | GLU | GLN | ||||
| 16 | ALA | GLY | GLU | ALA | GLU | ARG | LEU | ARG | ALA | TYR | ||||
| 17 | LEU | GLU | GLY | THR | CYS | VAL | GLU | TRP | LEU | ARG | ||||
| 18 | ARG | TYR | LEU | LYS | ASN | GLY | ASN | ALA | THR | LEU | ||||
| 19 | LEU | ARG | THR | ASP | SER | PRO | LYS | ALA | HIS | VAL | ||||
| 20 | THR | HIS | HIS | SER | ARG | PRO | GLU | ASP | LYS | VAL | ||||
| 21 | THR | LEU | ARG | CYS | TRP | ALA | LEU | GLY | PHE | TYR | ||||
| 22 | PRO | ALA | ASP | ILE | THR | LEU | THR | TRP | GLN | LEU | ||||
| 23 | ASN | GLY | GLU | GLU | LEU | ILE | GLN | ASP | MET | GLU | ||||
| 24 | LEU | VAL | GLU | THR | ARG | PRO | ALA | GLY | ASP | GLY | ||||
| 25 | THR | PHE | GLN | LYS | TRP | ALA | SER | VAL | VAL | VAL | ||||
| 26 | PRO | LEU | GLY | LYS | GLU | GLN | TYR | TYR | THR | CYS | ||||
| 27 | HIS | VAL | TYR | HIS | GLN | GLY | LEU | PRO | GLU | PRO | ||||
| 28 | LEU | THR | LEU | ARG | TRP | GLU | PRO | PRO | PRO | SER | ||||
| 29 | THR |
Entity 2, VSV8 8 residues - Formula weight is not available
| 1 | ARG | GLY | TYR | VAL | TYR | GLN | GLY | LEU |
Entity 3, b2m 99 residues - Formula weight is not available
| 1 | ILE | GLN | LYS | THR | PRO | GLN | ILE | GLN | VAL | TYR | ||||
| 2 | SER | ARG | HIS | PRO | PRO | GLU | ASN | GLY | LYS | PRO | ||||
| 3 | ASN | ILE | LEU | ASN | CYS | TYR | VAL | THR | GLN | PHE | ||||
| 4 | HIS | PRO | PRO | HIS | ILE | GLU | ILE | GLN | MET | LEU | ||||
| 5 | LYS | ASN | GLY | LYS | LYS | ILE | PRO | LYS | VAL | GLU | ||||
| 6 | MET | SER | ASP | MET | SER | PHE | SER | LYS | ASP | TRP | ||||
| 7 | SER | PHE | TYR | ILE | LEU | ALA | HIS | THR | GLU | PHE | ||||
| 8 | THR | PRO | THR | GLU | THR | ASP | THR | TYR | ALA | CYS | ||||
| 9 | ARG | VAL | LYS | HIS | ASP | SER | MET | ALA | GLU | PRO | ||||
| 10 | LYS | THR | VAL | TYR | TRP | ASP | ARG | ASP | MET |
Samples:
sample_1: H-2Kb, [U-13C; U-15N; U-2H], 400 uM; VSV8 400 uM; sodium phosphate 50 mM; sodium chloride 150 mM; b2m 400 mM
sample_conditions_1: ionic strength: 470 mM; pH: 7.0; 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-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
Cara, Keller - chemical shift assignment, data analysis, peak picking
RASP, MacRaild - chemical shift assignment
SPARTA+, Shen and Bax - chemical shift calculation
NMR spectrometers:
- Bruker UnityPlus 750 MHz
- Varian INOVA 600 MHz
- Bruker Avance 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks