BMRB Entry 18715
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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/BMR18715
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Title: Structure of HIV-1 myr(-) matrix protein in complex with 1,2-dioctanoyl-sn-phosphatidylcholine
Deposition date: 2012-09-14 Original release date: 2013-02-11
Authors: Vlach, Jiri; Saad, Jamil
Citation: Vlach, Jiri; Saad, Jamil. "Model for the interaction between HIV-1 Gag and plasma membrane" Proc. Natl. Acad. Sci. U.S.A. ., .-..
Assembly members:
MA, polymer, 131 residues, 14734.753 Da.
1,2-DIOCTANOYL-SN-GLYCERO-3-PHOSPHOCHOLINE, non-polymer, 510.622 Da.
Natural source: Common Name: HIV Taxonomy ID: 12721 Superkingdom: Viruses Kingdom: not available Genus/species: Lentivirus not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
MA: GARASVLSGGELDKWEKIRL
RPGGKKQYKLKHIVWASREL
ERFAVNPGLLETSEGCRQIL
GQLQPSLQTGSEELRSLYNT
IAVLYCVHQRIDVKDTKEAL
DKIEEEQNKSKKKAQQAAAD
TGNNSQVSQNY
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 434 |
15N chemical shifts | 131 |
1H chemical shifts | 880 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | MA | 1 |
2 | entity_PC8 | 2 |
Entities:
Entity 1, MA 131 residues - 14734.753 Da.
1 | GLY | ALA | ARG | ALA | SER | VAL | LEU | SER | GLY | GLY | ||||
2 | GLU | LEU | ASP | LYS | TRP | GLU | LYS | ILE | ARG | LEU | ||||
3 | ARG | PRO | GLY | GLY | LYS | LYS | GLN | TYR | LYS | LEU | ||||
4 | LYS | HIS | ILE | VAL | TRP | ALA | SER | ARG | GLU | LEU | ||||
5 | GLU | ARG | PHE | ALA | VAL | ASN | PRO | GLY | LEU | LEU | ||||
6 | GLU | THR | SER | GLU | GLY | CYS | ARG | GLN | ILE | LEU | ||||
7 | GLY | GLN | LEU | GLN | PRO | SER | LEU | GLN | THR | GLY | ||||
8 | SER | GLU | GLU | LEU | ARG | SER | LEU | TYR | ASN | THR | ||||
9 | ILE | ALA | VAL | LEU | TYR | CYS | VAL | HIS | GLN | ARG | ||||
10 | ILE | ASP | VAL | LYS | ASP | THR | LYS | GLU | ALA | LEU | ||||
11 | ASP | LYS | ILE | GLU | GLU | GLU | GLN | ASN | LYS | SER | ||||
12 | LYS | LYS | LYS | ALA | GLN | GLN | ALA | ALA | ALA | ASP | ||||
13 | THR | GLY | ASN | ASN | SER | GLN | VAL | SER | GLN | ASN | ||||
14 | TYR |
Entity 2, entity_PC8 - C24 H49 N O8 P - 510.622 Da.
1 | PC8 |
Samples:
sample_1: MA, [U-95% 13C], 0.4 mM; 1,2-DIOCTANOYL-SN-GLYCERO-3-PHOSPHOCHOLINE0.8 1.0 mM; sodium phosphate 50 mM; DTT 2 mM; H2O 90%; D2O 10%
sample_2: MA, [U-95% 13C; U-95% 15N], 0.4 1.0 mM; 1,2-DIOCTANOYL-SN-GLYCERO-3-PHOSPHOCHOLINE0.8 1.0 mM; sodium phosphate 50 mM; DTT 2 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 308 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 13C-edited/13C-filtered NOESY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_2 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CCPN_Analysis, CCPN - data analysis
NMR spectrometers:
- Bruker Avance II 700 MHz
Related Database Links:
EMBL | P12493 CBI61180 CBI61181 CBI61182 CBI61183 CBI61184 |
BMRB | 15114 15116 18716 |
PDB | |
DBJ | BAF34641 BAG48474 |
GB | AAA44987 AAB00898 AAB60571 AAC28445 AAC29216 |
SP | P12493 P12497 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts