BMRB Entry 27631
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27631
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: McShan, Andrew; Devlin, Christine; Overall, Sarah; Park, Jihye; Toor, Jugmohit; Moschidi, Danai; Flores-Solis, David; Choi, Hannah; Tripathi, Sarvind; Procko, Erik; Sgourakis, Nikolaos. "Molecular determinants of chaperone interactions on MHC-I for folding and antigen repertoire selection" Proc. Natl. Acad. Sci. U.S.A. 116, 25602-25613 (2019).
PubMed: 31796585
Assembly members:
HLA-A*02:01, polymer, 276 residues, Formula weight is not available
TAX_peptide, polymer, 9 residues, Formula weight is not available
human_beta2m, polymer, 100 residues, Formula weight is not available
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 Vector: pET
Entity Sequences (FASTA):
HLA-A*02:01: GSHSMRYFFTSVSRPGRGEP
RFIAVGYVDDTQFVRFDSDA
ASQRMEPRAPWIEQEGPEYW
DGETRKVKAHSQTHRVDLGT
LRGYYNQSEAGSHTVQRMYG
CDVGSDWRFLRGYHQYAYDG
KDYIALKEDLRSWTAADMAA
QTTKHKWEAAHVAEQLRAYL
EGTCVEWLRRYLENGKETLQ
RTDAPKTHMTHHAVSDHEAT
LRCWALSFYPAEITLTWQRD
GEDQTQDTELVETRPAGDGT
FQKWAAVVVPSGQEQRYTCH
VQHEGLPKPLTLRWEP
TAX_peptide: LLFGYPVYV
human_beta2m: MIQRTPKIQVYSRHPAENGK
SNFLNCYVSGFHPSDIEVDL
LKNGERIEKVEHSDLSFSKD
WSFYLLYYTEFTPTEKDEYA
CRVNHVTLSQPKIVKWDRDM
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 796 |
| 15N chemical shifts | 235 |
| 1H chemical shifts | 490 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Heavy chain | 1 |
| 2 | Peptide | 2 |
| 3 | Light chain | 3 |
Entities:
Entity 1, Heavy chain 276 residues - Formula weight is not available
| 1 | GLY | SER | HIS | SER | MET | ARG | TYR | PHE | PHE | THR | ||||
| 2 | SER | VAL | SER | ARG | PRO | GLY | ARG | GLY | GLU | PRO | ||||
| 3 | ARG | PHE | ILE | ALA | VAL | GLY | TYR | VAL | ASP | ASP | ||||
| 4 | THR | GLN | PHE | VAL | ARG | PHE | ASP | SER | ASP | ALA | ||||
| 5 | ALA | SER | GLN | ARG | MET | GLU | PRO | ARG | ALA | PRO | ||||
| 6 | TRP | ILE | GLU | GLN | GLU | GLY | PRO | GLU | TYR | TRP | ||||
| 7 | ASP | GLY | GLU | THR | ARG | LYS | VAL | LYS | ALA | HIS | ||||
| 8 | SER | GLN | THR | HIS | ARG | VAL | ASP | LEU | GLY | THR | ||||
| 9 | LEU | ARG | GLY | TYR | TYR | ASN | GLN | SER | GLU | ALA | ||||
| 10 | GLY | SER | HIS | THR | VAL | GLN | ARG | MET | TYR | GLY | ||||
| 11 | CYS | ASP | VAL | GLY | SER | ASP | TRP | ARG | PHE | LEU | ||||
| 12 | ARG | GLY | TYR | HIS | GLN | TYR | ALA | TYR | ASP | GLY | ||||
| 13 | LYS | ASP | TYR | ILE | ALA | LEU | LYS | GLU | ASP | LEU | ||||
| 14 | ARG | SER | TRP | THR | ALA | ALA | ASP | MET | ALA | ALA | ||||
| 15 | GLN | THR | THR | LYS | HIS | LYS | TRP | GLU | ALA | ALA | ||||
| 16 | HIS | VAL | ALA | GLU | GLN | LEU | ARG | ALA | TYR | LEU | ||||
| 17 | GLU | GLY | THR | CYS | VAL | GLU | TRP | LEU | ARG | ARG | ||||
| 18 | TYR | LEU | GLU | ASN | GLY | LYS | GLU | THR | LEU | GLN | ||||
| 19 | ARG | THR | ASP | ALA | PRO | LYS | THR | HIS | MET | THR | ||||
| 20 | HIS | HIS | ALA | VAL | SER | ASP | HIS | GLU | ALA | THR | ||||
| 21 | LEU | ARG | CYS | TRP | ALA | LEU | SER | PHE | TYR | PRO | ||||
| 22 | ALA | GLU | ILE | THR | LEU | THR | TRP | GLN | ARG | ASP | ||||
| 23 | GLY | GLU | ASP | GLN | THR | GLN | ASP | THR | GLU | LEU | ||||
| 24 | VAL | GLU | THR | ARG | PRO | ALA | GLY | ASP | GLY | THR | ||||
| 25 | PHE | GLN | LYS | TRP | ALA | ALA | VAL | VAL | VAL | PRO | ||||
| 26 | SER | GLY | GLN | GLU | GLN | ARG | TYR | THR | CYS | HIS | ||||
| 27 | VAL | GLN | HIS | GLU | GLY | LEU | PRO | LYS | PRO | LEU | ||||
| 28 | THR | LEU | ARG | TRP | GLU | PRO |
Entity 2, Peptide 9 residues - Formula weight is not available
| 1 | LEU | LEU | PHE | GLY | TYR | PRO | VAL | TYR | VAL |
Entity 3, Light chain 100 residues - Formula weight is not available
| 1 | MET | ILE | GLN | ARG | THR | PRO | LYS | ILE | GLN | VAL | |
| 2 | TYR | SER | ARG | HIS | PRO | ALA | GLU | ASN | GLY | LYS | |
| 3 | SER | ASN | PHE | LEU | ASN | CYS | TYR | VAL | SER | GLY | |
| 4 | PHE | HIS | PRO | SER | ASP | ILE | GLU | VAL | ASP | LEU | |
| 5 | LEU | LYS | ASN | GLY | GLU | ARG | ILE | GLU | LYS | VAL | |
| 6 | GLU | HIS | SER | ASP | LEU | SER | PHE | SER | LYS | ASP | |
| 7 | TRP | SER | PHE | TYR | LEU | LEU | TYR | TYR | THR | GLU | |
| 8 | PHE | THR | PRO | THR | GLU | LYS | ASP | GLU | TYR | ALA | |
| 9 | CYS | ARG | VAL | ASN | HIS | VAL | THR | LEU | SER | GLN | |
| 10 | PRO | LYS | ILE | VAL | LYS | TRP | ASP | ARG | ASP | MET |
Samples:
sample_1: HLA-A*02:01, [U-100% 13C; U-100% 15N], 500 uM; human beta2m 500 uM; TAX peptide 500 uM
sample_2: HLA-A*02:01, 13C AILV methyl, [U]-15N, 500 uM; TAX peptide 500 uM; human beta2m 500 uM
sample_conditions_1: ionic strength: 50 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks