BMRB Entry 19282
Click here to enlarge.
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/BMR19282
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: NMR structure of the lymphocyte receptor NKR-P1A
Deposition date: 2013-05-31 Original release date: 2014-06-09
Authors: Chmelik, Josef; Rozbesky, Daniel; Pospisilova, Eliska; Novak, Petr
Citation: Rozbesky, Daniel; Pospisilova, Eliska; Novak, Petr; Chmelik, Josef. "NMR structure of the lymphocyte receptor NKR-P1A reveals a different conformation of the conserved loop compared to crystal structure" Not known ., .-..
Assembly members:
NKR-P1A, polymer, 139 residues, 16008.889 Da.
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):
NKR-P1A: SAKLECPQDWLSHRDKCFHV
SQVSNTWEEGLVDCDGKGAT
LMLIQDQEELRFLLDSIKEK
YNSFWIGLRYTLPDMNWKWI
NGSTLNSDVLKITGDTENDS
CAAISGDKVTFESCNSDNRW
ICQKELYHETLSNYVGYGH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 622 |
| 15N chemical shifts | 157 |
| 1H chemical shifts | 967 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | lymphocyte receptor NKR-P1A | 1 |
Entities:
Entity 1, lymphocyte receptor NKR-P1A 139 residues - 16008.889 Da.
| 1 | SER | ALA | LYS | LEU | GLU | CYS | PRO | GLN | ASP | TRP | ||||
| 2 | LEU | SER | HIS | ARG | ASP | LYS | CYS | PHE | HIS | VAL | ||||
| 3 | SER | GLN | VAL | SER | ASN | THR | TRP | GLU | GLU | GLY | ||||
| 4 | LEU | VAL | ASP | CYS | ASP | GLY | LYS | GLY | ALA | THR | ||||
| 5 | LEU | MET | LEU | ILE | GLN | ASP | GLN | GLU | GLU | LEU | ||||
| 6 | ARG | PHE | LEU | LEU | ASP | SER | ILE | LYS | GLU | LYS | ||||
| 7 | TYR | ASN | SER | PHE | TRP | ILE | GLY | LEU | ARG | TYR | ||||
| 8 | THR | LEU | PRO | ASP | MET | ASN | TRP | LYS | TRP | ILE | ||||
| 9 | ASN | GLY | SER | THR | LEU | ASN | SER | ASP | VAL | LEU | ||||
| 10 | LYS | ILE | THR | GLY | ASP | THR | GLU | ASN | ASP | SER | ||||
| 11 | CYS | ALA | ALA | ILE | SER | GLY | ASP | LYS | VAL | THR | ||||
| 12 | PHE | GLU | SER | CYS | ASN | SER | ASP | ASN | ARG | TRP | ||||
| 13 | ILE | CYS | GLN | LYS | GLU | LEU | TYR | HIS | GLU | THR | ||||
| 14 | LEU | SER | ASN | TYR | VAL | GLY | TYR | GLY | HIS |
Samples:
sample: NKR-P1A, [U-100% 13C; U-100% 15N], 0.5 mM; PIPES 15 mM; sodium chloride 50 mM; sodium azide 1 mM; H2O 90%; D2O 10%
sample_conditions: pH: 6.8; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample | isotropic | sample_conditions |
| 2D 1H-13C HSQC aliphatic | sample | isotropic | sample_conditions |
| 3D CBCA(CO)NH | sample | isotropic | sample_conditions |
| 3D HNCACB | sample | isotropic | sample_conditions |
| 3D HNCA | sample | isotropic | sample_conditions |
| 3D HN(CO)CA | sample | isotropic | sample_conditions |
| 3D HNCO | sample | isotropic | sample_conditions |
| 3D HN(CA)CO | sample | isotropic | sample_conditions |
| 3D H(CCO)NH | sample | isotropic | sample_conditions |
| 3D (H)C(CO)NH | sample | isotropic | sample_conditions |
| 3D HCCH-TOCSY aliphatic | sample | isotropic | sample_conditions |
| 3D 1H-15N NOESY | sample | isotropic | sample_conditions |
| 2D 1H-13C HSQC aromatic | sample | isotropic | sample_conditions |
| 3D HCCH-TOCSY aromatic | sample | isotropic | sample_conditions |
| 2D (HB)CB(CGCD)HD | sample | isotropic | sample_conditions |
| 3D 1H-13C NOESY aliphatic | sample | isotropic | sample_conditions |
| 3D 1H-13C NOESY aromatic | sample | isotropic | sample_conditions |
Software:
TOPSPIN v2.3.6, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY v3.113, Goddard - chemical shift assignment, data analysis, peak picking
ARIA v2.3.1, Linge, O, . - structure solution
CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
RECOORD, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CING, (CING) Vuister, Doreleijer, da Silva - validation
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| EMBL | CAA45971 CAA45976 |
| GB | AAA39366 AAA39822 AAI20708 AAI45046 AAK39101 |
| REF | NP_001153374 NP_034867 |
| SP | P27811 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts