BMRB Entry 27682
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27682
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:
H-2Ld, polymer, 277 residues, Formula weight is not available
hb2m, polymer, 99 residues, Formula weight is not available
NIH_peptide, polymer, 9 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: pET
Entity Sequences (FASTA):
H-2Ld: MPHSMRYFETAVSRPGLGEP
RYISVGYVDNKEFVRFDSDA
ENPRYEPQAPWMEQEGPEYW
ERITQIAKGQEQWFRVNLRT
LLGYYNQSAGGTHTLQWMYG
CDVGSDGRLLRGYEQFAYDG
CDYIALNEDLKTWTAADMAA
QITRRKWEQAGAAEYYRAYL
EGECVEWLHRYLKNGNATLL
RTDSPKAHVTHHPRSKGEVT
LRCWALGFYPADITLTWQLN
GEELTQDMELVETRPAGDGT
FQKWASVVVPLGKEQNYTCR
VYHEGLPEPLTLRWEPP
hb2m: IQRTPKIQVYSRHPAENGKS
NFLNCYVSGFHPSDIEVDLL
KNGERIEKVEHSDLSFSKDW
SFYLLYYTEFTPTEKDEYAC
RVNHVTLSQPKIVKWDRDM
NIH_peptide: YPNVNIHNF
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 765 |
| 15N chemical shifts | 235 |
| 1H chemical shifts | 464 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | H-2Ld | 1 |
| 2 | hb2m | 2 |
| 3 | NIH | 3 |
Entities:
Entity 1, H-2Ld 277 residues - Formula weight is not available
| 1 | MET | PRO | HIS | SER | MET | ARG | TYR | PHE | GLU | THR | ||||
| 2 | ALA | VAL | SER | ARG | PRO | GLY | LEU | GLY | GLU | PRO | ||||
| 3 | ARG | TYR | ILE | SER | VAL | GLY | TYR | VAL | ASP | ASN | ||||
| 4 | LYS | GLU | PHE | VAL | ARG | PHE | ASP | SER | ASP | ALA | ||||
| 5 | GLU | ASN | PRO | ARG | TYR | GLU | PRO | GLN | ALA | PRO | ||||
| 6 | TRP | MET | GLU | GLN | GLU | GLY | PRO | GLU | TYR | TRP | ||||
| 7 | GLU | ARG | ILE | THR | GLN | ILE | ALA | LYS | GLY | GLN | ||||
| 8 | GLU | GLN | TRP | PHE | ARG | VAL | ASN | LEU | ARG | THR | ||||
| 9 | LEU | LEU | GLY | TYR | TYR | ASN | GLN | SER | ALA | GLY | ||||
| 10 | GLY | THR | HIS | THR | LEU | GLN | TRP | MET | TYR | GLY | ||||
| 11 | CYS | ASP | VAL | GLY | SER | ASP | GLY | ARG | LEU | LEU | ||||
| 12 | ARG | GLY | TYR | GLU | GLN | PHE | ALA | TYR | ASP | GLY | ||||
| 13 | CYS | ASP | TYR | ILE | ALA | LEU | ASN | GLU | ASP | LEU | ||||
| 14 | LYS | THR | TRP | THR | ALA | ALA | ASP | MET | ALA | ALA | ||||
| 15 | GLN | ILE | THR | ARG | ARG | LYS | TRP | GLU | GLN | ALA | ||||
| 16 | GLY | ALA | ALA | GLU | TYR | TYR | ARG | ALA | TYR | LEU | ||||
| 17 | GLU | GLY | GLU | CYS | VAL | GLU | TRP | LEU | HIS | ARG | ||||
| 18 | TYR | LEU | LYS | ASN | GLY | ASN | ALA | THR | LEU | LEU | ||||
| 19 | ARG | THR | ASP | SER | PRO | LYS | ALA | HIS | VAL | THR | ||||
| 20 | HIS | HIS | PRO | ARG | SER | LYS | GLY | GLU | VAL | THR | ||||
| 21 | LEU | ARG | CYS | TRP | ALA | LEU | GLY | PHE | TYR | PRO | ||||
| 22 | ALA | ASP | ILE | THR | LEU | THR | TRP | GLN | LEU | ASN | ||||
| 23 | GLY | GLU | GLU | LEU | THR | GLN | ASP | MET | GLU | LEU | ||||
| 24 | VAL | GLU | THR | ARG | PRO | ALA | GLY | ASP | GLY | THR | ||||
| 25 | PHE | GLN | LYS | TRP | ALA | SER | VAL | VAL | VAL | PRO | ||||
| 26 | LEU | GLY | LYS | GLU | GLN | ASN | TYR | THR | CYS | ARG | ||||
| 27 | VAL | TYR | HIS | GLU | GLY | LEU | PRO | GLU | PRO | LEU | ||||
| 28 | THR | LEU | ARG | TRP | GLU | PRO | PRO |
Entity 2, hb2m 99 residues - Formula weight is not available
| 1 | ILE | GLN | ARG | THR | PRO | LYS | ILE | GLN | VAL | TYR | ||||
| 2 | SER | ARG | HIS | PRO | ALA | GLU | ASN | GLY | LYS | SER | ||||
| 3 | ASN | PHE | LEU | ASN | CYS | TYR | VAL | SER | GLY | PHE | ||||
| 4 | HIS | PRO | SER | ASP | ILE | GLU | VAL | ASP | LEU | LEU | ||||
| 5 | LYS | ASN | GLY | GLU | ARG | ILE | GLU | LYS | VAL | GLU | ||||
| 6 | HIS | SER | ASP | LEU | SER | PHE | SER | LYS | ASP | TRP | ||||
| 7 | SER | PHE | TYR | LEU | LEU | TYR | TYR | THR | GLU | PHE | ||||
| 8 | THR | PRO | THR | GLU | LYS | ASP | GLU | TYR | ALA | CYS | ||||
| 9 | ARG | VAL | ASN | HIS | VAL | THR | LEU | SER | GLN | PRO | ||||
| 10 | LYS | ILE | VAL | LYS | TRP | ASP | ARG | ASP | MET |
Entity 3, NIH 9 residues - Formula weight is not available
| 1 | TYR | PRO | ASN | VAL | ASN | ILE | HIS | ASN | PHE |
Samples:
sample_CND_H-2Ld: H-2Ld, [U-13C; U-15N; U-2H], 0.4 mM
sample_AILV_H_2Ld: H-2Ld, Ala 13C ; Ile 13C 1; Leu 13C 1/13C 2; Val 13C 1/13C 2) U-[15N, 2H, 0.6 mM
sample_conditions_CND_H-2Ld: ionic strength: 0.05 M; pH: 6.4; pressure: 1 atm; temperature: 298 K
sample_conditions_AILV_H_2Ld: ionic strength: 0.05 M; pH: 7.2; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_CND_H-2Ld | isotropic | sample_conditions_CND_H-2Ld |
| 3D HNCA | sample_CND_H-2Ld | isotropic | sample_conditions_CND_H-2Ld |
| 3D HNCB | sample_CND_H-2Ld | isotropic | sample_conditions_CND_H-2Ld |
| 3D 1H-13C NOESY | sample_AILV_H_2Ld | isotropic | sample_conditions_AILV_H_2Ld |
| 3D 1H-15N NOESY | sample_AILV_H_2Ld | isotropic | sample_conditions_AILV_H_2Ld |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
- 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