BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17216

Title: How the HIV-1 Nucleocapsid Protein Binds and Destabilises the (-)Primer Binding Site During Reverse Transcription   PubMed: 18773912

Deposition date: 2010-09-29 Original release date: 2010-11-10

Authors: Bourbigot, Sarah; Ramalanjaona, Nick; Boudier, Christian; Salgado, Gilmar; Roques, Bernard; Mely, Yves; Bouaziz, Serge; Morellet, Nelly

Citation: Bourbigot, Sarah; Ramalanjaona, Nick; Boudier, Christian; Salgado, Gilmar; Roques, Bernard; Mely, Yves; Bouaziz, Serge; Morellet, Nelly. "How the HIV-1 Nucleocapsid Protein Binds and Destabilises the (-)Primer Binding Site During Reverse Transcription"  J. Mol. Biol. 383, 1112-1128 (2008).

Assembly members:
PPBS, polymer, 12 residues, Formula weight is not available
NCp7(12-55), polymer, 44 residues, Formula weight is not available

Natural source:   Common Name: Human immunodeficiency virus 1   Taxonomy ID: 11676   Superkingdom: not available   Kingdom: not available   Genus/species: Lentivirus not available

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
PPBS: GCCCTGTTGGGC
NCp7(12-55): NVKCFNCGKEGHTARNCRAP RKKGCWKCGKEGHQMKDCTE RQAN

Data sets:
Data typeCount
kinetic rates4

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1PPBS1
2NCp7(12-55)2

Entities:

Entity 1, PPBS 12 residues - Formula weight is not available

1   DGDCDCDCDTDGDTDTDGDG
2   DGDC

Entity 2, NCp7(12-55) 44 residues - Formula weight is not available

1   ASNVALLYSCYSPHEASNCYSGLYLYSGLU
2   GLYHISTHRALAARGASNCYSARGALAPRO
3   ARGLYSLYSGLYCYSTRPLYSCYSGLYLYS
4   GLUGLYHISGLNMETLYSASPCYSTHRGLU
5   ARGGLNALAASN

Samples:

sample_1: PPBS 1 mM; NCp7(12-55) 1 mM; D2O 100%

sample_2: PPBS 1 mM; NCp7(12-55) 1 mM; D2O 10%; H2O 90%

sample_conditions_1: pH: 6.5; pressure: ambient atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D EXSYsample_1isotropicsample_conditions_1
2D EXSYsample_2isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - processing

FELIX, Accelrys Software Inc. - processing

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 2217 25532
PDB
DBJ BAA12988 BAA12996 BAB85751 BAB85752 BAC02530
EMBL CAB58976 CAB58988 CAB98186 CAP69989 CAP69993
GB AAA44201 AAA45076 AAA76686 AAB05598 AAB21888
PIR FOVWLV
PRF 1102247B 1103299C
REF NP_057849 NP_057850 NP_579881
SP P03347 P03348 P03366 P03367 P04585