BMRB Entry 16555
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16555
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Title: 1H, 15N and 13C assignments of the dimeric C-terminal domain of HIV-1 capsid protein PubMed: 19921549
Deposition date: 2009-10-15 Original release date: 2009-11-30
Authors: Jung, Jinwon; Byeon, In-Ja; Ahn, Jinwoo; Concel, Jason; Gronenborn, Angela
Citation: Jung, Jinwon; Byeon, In-Ja; Ahn, Jinwoo; Concel, Jason; Gronenborn, Angela. "1H, 15N and 13C assignments of the dimeric C-terminal domain of HIV-1 capsid protein." Biomol. NMR Assignments 4, 21-23 (2010).
Assembly members:
HIV-1_Capsid_Protein, polymer, 88 residues, Formula weight is not available
Natural source: Common Name: Lentivirus human immunodeficiency virus Taxonomy ID: 11646 Superkingdom: Viruses Kingdom: not available Genus/species: Lentivirus HIV-1
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
HIV-1_Capsid_Protein: MYSPTSILDIRQGPKEPFRD
YVDRFYKTLRAEQASQEVKN
WMTETLLVQNANPDCKTILK
ALGPAATLEEMMTACQGVGG
PGHKARVL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 272 |
| 15N chemical shifts | 91 |
| 1H chemical shifts | 568 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | subunit 1 | 1 |
| 2 | subunit 2 | 1 |
Entities:
Entity 1, subunit 1 88 residues - Formula weight is not available
| 1 | MET | TYR | SER | PRO | THR | SER | ILE | LEU | ASP | ILE | ||||
| 2 | ARG | GLN | GLY | PRO | LYS | GLU | PRO | PHE | ARG | ASP | ||||
| 3 | TYR | VAL | ASP | ARG | PHE | TYR | LYS | THR | LEU | ARG | ||||
| 4 | ALA | GLU | GLN | ALA | SER | GLN | GLU | VAL | LYS | ASN | ||||
| 5 | TRP | MET | THR | GLU | THR | LEU | LEU | VAL | GLN | ASN | ||||
| 6 | ALA | ASN | PRO | ASP | CYS | LYS | THR | ILE | LEU | LYS | ||||
| 7 | ALA | LEU | GLY | PRO | ALA | ALA | THR | LEU | GLU | GLU | ||||
| 8 | MET | MET | THR | ALA | CYS | GLN | GLY | VAL | GLY | GLY | ||||
| 9 | PRO | GLY | HIS | LYS | ALA | ARG | VAL | LEU |
Samples:
sample_1: HIV-1 CA-CTD, [U-100% 13C; U-100% 15N], 2 mM; H2O 93%; D2O 7%; sodium phosphate 25 mM; sodium azide 0.02%; DTT 2 mM
sample_conditions_1: ionic strength: 25 mM; pH: 6.5; 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | 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 HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D simultaneous 13C,15N-edited NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-edited NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment
NMRView, Johnson, One Moon Scientific - data analysis
NMR spectrometers:
- Bruker Avance 900 MHz
- Bruker Avance 800 MHz
- Bruker Avance 700 MHz
Related Database Links:
| BMRB | 15137 17307 19261 19575 25532 |
| PDB | |
| DBJ | BAA00992 BAA12988 BAA12996 BAA93773 BAA93774 |
| EMBL | CAA06946 CAA11880 CAA11884 CAA11886 CAA12915 |
| GB | AAA44201 AAA44224 AAA44225 AAA44306 AAA44652 |
| 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