BMRB Entry 17307
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17307
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Title: NMR Structure of the monomeric mutant C-terminal domain of HIV-1 Capsid in complex with stapled peptide Inhibitor PubMed: 18417468
Deposition date: 2010-11-18 Original release date: 2010-12-16
Authors: Bhattacharya, Shibani; Zhang, Hongtao; Debnath, Asim; Cowburn, David
Citation: Bhattacharya, Shibani; Zhang, Hongtao; Debnath, Asim; Cowburn, David. "Solution structure of a hydrocarbon stapled peptide inhibitor in complex with monomeric C-terminal domain of HIV-1 capsid." J. Biol. Chem. 283, 16247-16278 (2008).
Assembly members:
Capsid_protein_p24, polymer, 105 residues, Formula weight is not available
NYAD-13_Peptide_Inhibitor, polymer, 14 residues, Formula weight is not available
Natural source: Common Name: HIV-1 Taxonomy ID: 11676 Superkingdom: virus Kingdom: not available Genus/species: Lentivirus not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Capsid_protein_p24: MGSSHHHHHHSSGLVPRGSH
MTSILDIRQGPKEPFRDYVD
RFYKTLRAEQASQEVKNAAT
ETLLVQNANPDCKTILKALG
PAATLEEMMTACQGVGGPGH
KARVL
NYAD-13_Peptide_Inhibitor: ITFXDLLXYYGKKK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 377 |
| 15N chemical shifts | 94 |
| 1H chemical shifts | 713 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Capsid_protein_p24 | 1 |
| 2 | NYAD-13_Peptide_Inhibitor | 2 |
Entities:
Entity 1, Capsid_protein_p24 105 residues - Formula weight is not available
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | THR | SER | ILE | LEU | ASP | ILE | ARG | GLN | GLY | ||||
| 4 | PRO | LYS | GLU | PRO | PHE | ARG | ASP | TYR | VAL | ASP | ||||
| 5 | ARG | PHE | TYR | LYS | THR | LEU | ARG | ALA | GLU | GLN | ||||
| 6 | ALA | SER | GLN | GLU | VAL | LYS | ASN | ALA | ALA | THR | ||||
| 7 | GLU | THR | LEU | LEU | VAL | GLN | ASN | ALA | ASN | PRO | ||||
| 8 | ASP | CYS | LYS | THR | ILE | LEU | LYS | ALA | LEU | GLY | ||||
| 9 | PRO | ALA | ALA | THR | LEU | GLU | GLU | MET | MET | THR | ||||
| 10 | ALA | CYS | GLN | GLY | VAL | GLY | GLY | PRO | GLY | HIS | ||||
| 11 | LYS | ALA | ARG | VAL | LEU |
Entity 2, NYAD-13_Peptide_Inhibitor 14 residues - Formula weight is not available
X=MK8 cis double bond between CE atoms of residue 4 and 8.
| 1 | ILE | THR | PHE | MK8 | ASP | LEU | LEU | MK8 | TYR | TYR | ||||
| 2 | GLY | LYS | LYS | LYS |
Samples:
sample_1: Capsid protein p24, [U-100% 13C; U-100% 15N], 600 uM; NYAD-13 Peptide Inhibitor 900 uM; DTT 2 mM; ammonium acetate 100 mM; H2O 90%; D2O 10%
sample_2: Capsid protein p24, [U-100% 13C; U-100% 15N], 600 uM; NYAD-13 Peptide Inhibitor 900 uM; DTT 2 mM; ammonium acetate 100 mM; D2O 100%
sample_conditions_1: ionic strength: 100 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-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D f1,f2 filtered 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D f2 filtered 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
ARIA v2.2, Linge, O, . - refinement
CARA v1.5, Keller, Wuthrich - chemical shift assignment, peak picking
TOPSPIN v1.3, Bruker Biospin - processing
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 900 MHz
Related Database Links:
| BMRB | 15137 16555 17738 19264 25532 |
| PDB | |
| DBJ | BAA00992 BAA12988 BAA12996 BAA93785 BAA93786 |
| EMBL | CAA82791 CAA82793 CAB85858 CAB85866 CAB87157 |
| GB | AAA44201 AAA44306 AAA44652 AAA76686 AAB04036 |
| PIR | FOVWLV |
| PRF | 1102247B 1103299C |
| REF | NP_057849 NP_057850 NP_579880 |
| SP | P03347 P03348 P03366 P03367 P04585 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts