BMRB Entry 15137
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15137
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Title: The solution structure of the monomeric species of the C terminal domain of the CA protein of HIV-1 PubMed: 17526561
Deposition date: 2007-02-17 Original release date: 2007-10-24
Authors: Alcaraz, Luis; del Alamo, Marta; Barrera, Francisco; Mateu, Mauricio; Neira, Jose
Citation: Alcaraz, Luis; del Alamo, Marta; Barrera, Francisco; Mateu, Mauricio; Neira, Jose. "Flexibility in HIV-1 assembly units: solution structure and dynamics of the monomeric C-terminal domain of the capsid protein" Biophys. J. 93, 1264-1276 (2007).
Assembly members:
CAC monomer, polymer, 87 residues, 9567.128 Da.
Natural source: Common Name: HIV Taxonomy ID: 11676 Superkingdom: Viruses Kingdom: not available Genus/species: Lentivirus HIV
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
CAC monomer: MSPTSILDIRQGPKEPFRDY
VDRFYKTLRAEQASQEVKNA
MTETLLVQNANPDCKTILKA
LGPAATLEEMMTACQGVGGP
GHKARVL
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 68 |
| 1H chemical shifts | 526 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CAC monomer | 1 |
Entities:
Entity 1, CAC monomer 87 residues - 9567.128 Da.
| 1 | MET | SER | PRO | THR | SER | ILE | LEU | ASP | ILE | ARG | ||||
| 2 | GLN | GLY | PRO | LYS | GLU | PRO | PHE | ARG | ASP | TYR | ||||
| 3 | VAL | ASP | ARG | PHE | TYR | LYS | THR | LEU | ARG | ALA | ||||
| 4 | GLU | GLN | ALA | SER | GLN | GLU | VAL | LYS | ASN | ALA | ||||
| 5 | MET | THR | GLU | THR | LEU | LEU | VAL | GLN | ASN | ALA | ||||
| 6 | ASN | PRO | ASP | CYS | LYS | THR | ILE | LEU | LYS | ALA | ||||
| 7 | LEU | GLY | PRO | ALA | ALA | THR | LEU | GLU | GLU | MET | ||||
| 8 | MET | THR | ALA | CYS | GLN | GLY | VAL | GLY | GLY | PRO | ||||
| 9 | GLY | HIS | LYS | ALA | ARG | VAL | LEU |
Samples:
sample_1: entity, [U-15N], 1 mM; potassium phosphate, none, 100 mM; TSP, none, 0.00001 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, P Guntert, C Mumenthaler and K Wuthrich - structure solution
SPARKY v3.0, T Goddard - chemical shift assignment, peak picking
AMBER v8, DA Case, TA Darden, TE Cheatham, III, CL Simmerling, J Wang, RE Duke, - refinement
xwinnmr, Bruker Biospin - collection
NMR spectrometers:
- Bruker DRX 500 MHz
Related Database Links:
| BMRB | 16555 17307 17738 19261 19264 19575 25532 |
| PDB | |
| DBJ | BAA00992 BAA12988 BAA12996 BAA93773 BAA93774 |
| EMBL | CAA06946 CAA11880 CAA11886 CAA77621 CAA82791 |
| GB | AAA44201 AAA44306 AAA44652 AAA44987 AAA45003 |
| PIR | FOVWLV |
| PRF | 1102247B 1103299C |
| REF | NP_057849 NP_057850 NP_579880 |
| SP | P03347 P03348 P03349 P03366 P03367 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts