BMRB Entry 16887

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16887
MolProbity Validation Chart

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Title:
Backbone 1H, 13C, 15N Chemical Shift Assignments for HIV-2 unmyristoylated matrix protein
Deposition date:
2010-04-21
Original release date:
2010-08-12
Authors:
Saad, Jamil; Ablan, Sherimay; Ghanam, Ruba; Kim, Andrew; Andrews, Kalola; Nagashima, Kunio; Freed, Eric; Summers, Michael
Citation:

Citation: Saad, Jamil; Ablan, Sherimay; Ghanam, Ruba; Kim, Andrew; Andrews, Kalola; Nagashima, Kunio; Soheilian, Ferri; Freed, Eric; Summers, Michael. "Structure of the myristylated human immunodeficiency virus type 2 matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in membrane targeting."  J. Mol. Biol. 382, 434-447 (2008).
PubMed: 18657545

Assembly members:

Assembly members:
HIV2, polymer, 134 residues, 14899.383 Da.

Natural source:

Natural source:   Common Name: Human immunodeficiency virus 2   Taxonomy ID: 11709   Superkingdom: virus   Kingdom: not available   Genus/species: Lentivirus HIV2

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET16b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HIV2: GARNSVLRGKKADELERIRL RPGGKKKYRLKHIVWAANKL DRFGLAESLLESKEGCQKIL TVLDPMVPTGSENLKSLFNT VCVIWCIHAEEKVKDTEGAK QIVRRHLVAETGTAEKMPST SRPTAPSSEKGGNY

Data sets:
Data typeCount
13C chemical shifts380
15N chemical shifts126
1H chemical shifts737

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1HIV-2 unmyristoylated matrix protein1

Entities:

Entity 1, HIV-2 unmyristoylated matrix protein 134 residues - 14899.383 Da.

1   GLYALAARGASNSERVALLEUARGGLYLYS
2   LYSALAASPGLULEUGLUARGILEARGLEU
3   ARGPROGLYGLYLYSLYSLYSTYRARGLEU
4   LYSHISILEVALTRPALAALAASNLYSLEU
5   ASPARGPHEGLYLEUALAGLUSERLEULEU
6   GLUSERLYSGLUGLYCYSGLNLYSILELEU
7   THRVALLEUASPPROMETVALPROTHRGLY
8   SERGLUASNLEULYSSERLEUPHEASNTHR
9   VALCYSVALILETRPCYSILEHISALAGLU
10   GLULYSVALLYSASPTHRGLUGLYALALYS
11   GLNILEVALARGARGHISLEUVALALAGLU
12   THRGLYTHRALAGLULYSMETPROSERTHR
13   SERARGPROTHRALAPROSERSERGLULYS
14   GLYGLYASNTYR

Samples:

sample_1: HIV-2 unmyristoylated matrix protein, [U-15N], 0.8 mM; potassium phosphate 20 mM; DTT 10 mM; Glutamate 50 mM; Aspartate 50 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_2: HIV-2 unmyristoylated matrix protein 0.8 mM; potassium phosphate 20 mM; DTT 10 mM; Glutamate 50 mM; Aspartate 50 mM; sodium chloride 100 mM; D2O 100%

sample_3: HIV-2 unmyristoylated matrix protein, [U-13C; U-15N], 0.8 mM; potassium phosphate 20 mM; DTT 10 mM; Glutamate 50 mM; Aspartate 50 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.3; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

NMR spectrometers:

  • Bruker DRX 800 MHz
  • Bruker DMX 600 MHz

Related Database Links:

BMRB 16888 16889
PDB
EMBL CAA28909
GB AAB00763
PRF 1306388A
SP P04584 P04590
AlphaFold P04584 P04590

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks