BMRB Entry 17819
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17819
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Title: Backbone 1H, 13C, 15N assignment of Hck kinase regulatory segment complex with full length Nef PubMed: 21365684
Deposition date: 2011-07-29 Original release date: 2014-04-23
Authors: Jung, Jinwon; Byeon, In-Ja; Ahn, Jinwoo; Gronenborn, Angela
Citation: Jung, Jinwon; Byeon, In-Ja; Ahn, Jinwoo; Gronenborn, Angela. "Structure, dynamics, and Hck interaction of full-length HIV-1 Nef." Proteins 79, 1609-1622 (2011).
Assembly members:
Hck32L, polymer, 193 residues, Formula weight is not available
Nef, polymer, 217 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
Entity Sequences (FASTA):
Hck32L: GIREAGSEDIIVVALYDYEA
IHHEDLSFQKGDQMVVLEES
GEWWKARSLATRKEGYIPSN
YVARVDSLETEEWFFKGISR
KDAERQLLAPGNMLGSFMIR
DSETTKGSYSLSVRDYDPRQ
GDTVKHYKIRTLDNGGFYIS
PRSTFSTLQELVDHYKKGND
GLCQKLSVPCMSSKPQKPWE
KDAWELEHHHHHH
Nef: MEGKWSKRSVSGWPAVRERM
RRAEPAAEGVGAVSRDLEKH
GAITSSNTAATNAACAWLEA
QEEEEVGFPVRPQVPLRPMT
YKAAVDLSHFLKEKGGLEGL
IYSQKRQDILDLWVYHTQGY
FPDWQNYTPGPGIRYPLTFG
WCFKLVPVEPEKVEEANEGE
NNCLLHPMSQHGMDDPEKEV
LVWKFDSKLAFHHMARELHP
EYYKDCAAALEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 259 |
| 15N chemical shifts | 146 |
| 1H chemical shifts | 146 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Hck32L | 1 |
| 2 | Nef | 2 |
Entities:
Entity 1, Hck32L 193 residues - Formula weight is not available
This construct is 72-256 of Hck kinase. Last 8 residues (LEHHHHHH) are a histag.
| 1 | GLY | ILE | ARG | GLU | ALA | GLY | SER | GLU | ASP | ILE | ||||
| 2 | ILE | VAL | VAL | ALA | LEU | TYR | ASP | TYR | GLU | ALA | ||||
| 3 | ILE | HIS | HIS | GLU | ASP | LEU | SER | PHE | GLN | LYS | ||||
| 4 | GLY | ASP | GLN | MET | VAL | VAL | LEU | GLU | GLU | SER | ||||
| 5 | GLY | GLU | TRP | TRP | LYS | ALA | ARG | SER | LEU | ALA | ||||
| 6 | THR | ARG | LYS | GLU | GLY | TYR | ILE | PRO | SER | ASN | ||||
| 7 | TYR | VAL | ALA | ARG | VAL | ASP | SER | LEU | GLU | THR | ||||
| 8 | GLU | GLU | TRP | PHE | PHE | LYS | GLY | ILE | SER | ARG | ||||
| 9 | LYS | ASP | ALA | GLU | ARG | GLN | LEU | LEU | ALA | PRO | ||||
| 10 | GLY | ASN | MET | LEU | GLY | SER | PHE | MET | ILE | ARG | ||||
| 11 | ASP | SER | GLU | THR | THR | LYS | GLY | SER | TYR | SER | ||||
| 12 | LEU | SER | VAL | ARG | ASP | TYR | ASP | PRO | ARG | GLN | ||||
| 13 | GLY | ASP | THR | VAL | LYS | HIS | TYR | LYS | ILE | ARG | ||||
| 14 | THR | LEU | ASP | ASN | GLY | GLY | PHE | TYR | ILE | SER | ||||
| 15 | PRO | ARG | SER | THR | PHE | SER | THR | LEU | GLN | GLU | ||||
| 16 | LEU | VAL | ASP | HIS | TYR | LYS | LYS | GLY | ASN | ASP | ||||
| 17 | GLY | LEU | CYS | GLN | LYS | LEU | SER | VAL | PRO | CYS | ||||
| 18 | MET | SER | SER | LYS | PRO | GLN | LYS | PRO | TRP | GLU | ||||
| 19 | LYS | ASP | ALA | TRP | GLU | LEU | GLU | HIS | HIS | HIS | ||||
| 20 | HIS | HIS | HIS |
Entity 2, Nef 217 residues - Formula weight is not available
| 1 | MET | GLU | GLY | LYS | TRP | SER | LYS | ARG | SER | VAL | ||||
| 2 | SER | GLY | TRP | PRO | ALA | VAL | ARG | GLU | ARG | MET | ||||
| 3 | ARG | ARG | ALA | GLU | PRO | ALA | ALA | GLU | GLY | VAL | ||||
| 4 | GLY | ALA | VAL | SER | ARG | ASP | LEU | GLU | LYS | HIS | ||||
| 5 | GLY | ALA | ILE | THR | SER | SER | ASN | THR | ALA | ALA | ||||
| 6 | THR | ASN | ALA | ALA | CYS | ALA | TRP | LEU | GLU | ALA | ||||
| 7 | GLN | GLU | GLU | GLU | GLU | VAL | GLY | PHE | PRO | VAL | ||||
| 8 | ARG | PRO | GLN | VAL | PRO | LEU | ARG | PRO | MET | THR | ||||
| 9 | TYR | LYS | ALA | ALA | VAL | ASP | LEU | SER | HIS | PHE | ||||
| 10 | LEU | LYS | GLU | LYS | GLY | GLY | LEU | GLU | GLY | LEU | ||||
| 11 | ILE | TYR | SER | GLN | LYS | ARG | GLN | ASP | ILE | LEU | ||||
| 12 | ASP | LEU | TRP | VAL | TYR | HIS | THR | GLN | GLY | TYR | ||||
| 13 | PHE | PRO | ASP | TRP | GLN | ASN | TYR | THR | PRO | GLY | ||||
| 14 | PRO | GLY | ILE | ARG | TYR | PRO | LEU | THR | PHE | GLY | ||||
| 15 | TRP | CYS | PHE | LYS | LEU | VAL | PRO | VAL | GLU | PRO | ||||
| 16 | GLU | LYS | VAL | GLU | GLU | ALA | ASN | GLU | GLY | GLU | ||||
| 17 | ASN | ASN | CYS | LEU | LEU | HIS | PRO | MET | SER | GLN | ||||
| 18 | HIS | GLY | MET | ASP | ASP | PRO | GLU | LYS | GLU | VAL | ||||
| 19 | LEU | VAL | TRP | LYS | PHE | ASP | SER | LYS | LEU | ALA | ||||
| 20 | PHE | HIS | HIS | MET | ALA | ARG | GLU | LEU | HIS | PRO | ||||
| 21 | GLU | TYR | TYR | LYS | ASP | CYS | ALA | ALA | ALA | LEU | ||||
| 22 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: Hck32L, [U-13C; U-15N; U-2H], 0.5 mM; H2O 95%; D2O 5%; DTT 10 mM; HEPES 10 mM; sodium chloride 100 mM; sodium azide 0.02 w/v; Nef 0.6 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 8.0; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN v2.1, Bruker Biospin - collection
CARA v1.8.4, Rochus Keller - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker Avance 700 MHz
Related Database Links:
| UNP | P08631 |
| BMRB | 17740 17922 |
| PDB | |
| DBJ | BAB15482 BAF82585 BAF83617 BAG60878 |
| EMBL | CAC44031 |
| GB | AAA52643 AAA52644 AAH14435 AAH94847 AAI08931 AAA03700 |
| REF | NP_001165600 NP_001165601 NP_001165602 NP_001165603 NP_001165604 |
| SP | P08631 Q95M30 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts