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 7342

Title: SOLUTION STRUCTURE OF THE ZN COMPLEX OF HIV-2 NCP(23-49) PEPTIDE, ENCOMPASSING PROTEIN CCHC-LINKER, DISTAL CCHC ZN-BINDING MOTIF AND C-TERMINAL TAIL

Deposition date: 2006-12-01 Original release date: 2011-05-26

Authors: Amodeo, P.; Castiglione Morelli, M.; Ostuni, A.; Cristinziano, P.; Bavoso, A.

Citation: Amodeo, P.; Castiglione Morelli, M.; Ostuni, A.; Cristinziano, P.; Bavoso, A.. "Structural Features of the C-Terminal Zinc Finger Domain of the HIV-2 Nc Protein (Residues 23-49)."  .

Assembly members:
NUCLEOCAPSID_PROTEIN, polymer, 27 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

Natural source:   Common Name: HIV-2   Taxonomy ID: 11709   Superkingdom: Viruses   Kingdom: not available   Genus/species: Lentivirus HIV-2

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
NUCLEOCAPSID_PROTEIN: RAPRRQGCWKCGKTGHVMAK CPERQAG

Data sets:
Data typeCount
1H chemical shifts184

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NUCLEOCAPSID PROTEIN1
2ZINC ION2

Entities:

Entity 1, NUCLEOCAPSID PROTEIN 27 residues - Formula weight is not available

1   ARGALAPROARGARGGLNGLYCYSTRPLYS
2   CYSGLYLYSTHRGLYHISVALMETALALYS
3   CYSPROGLUARGGLNALAGLY

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample: NCp8 2.6 mM; H2O 80%; D2O 20%; TCEP.HCl 11.5 mM; zinc chloride 3.1 mM

sample_conditions_1: ionic strength: 130 mM; pH: 7.0; pressure: 1.0 atm; temperature: 298.0 K

Experiments:

NameSampleSample stateSample conditions
2D NOESYsampleisotropicsample_conditions_1
2D DQF-COSYsampleisotropicsample_conditions_1
2D TOCSYsampleisotropicsample_conditions_1

Software:

AMBER, PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM, FERGUSON,SEIBEL,SINGH,WEINER,KOLLMAN - refinement, structure solution

Molmol v2K.2 - data analysis

VNMR v6.1C - processing

NMR spectrometers:

  • VARIAN UNITYINOVA 500 MHz

Related Database Links:

BMRB 15196 15364 7384
PDB
EMBL CAA32483
GB AAA43932 AAB41427 AAC68655 AAL18230 ADI24350
PRF 1509334A
SP P12496 P12502 P18041 P18042
AlphaFold P18041 P12496 P12502 P18042