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 15137

Title: The solution structure of the monomeric species of the C terminal domain of the CA protein of HIV-1   PubMed: 17526561

Authors: Alcaraz, Luis; del Alamo, Marta; Barrera, Francisco; Mateu, Mauricio; Neira, Jose

Citation: Alcaraz, Luis; del Alamo, Marta; Barrera, Francisco; Mateu, Mauricio; Neira, Jose. "Flexibility in HIV-1 assembly units: solution structure and dynamics of the monomeric C-terminal domain of the capsid protein"  Biophys. J. 93, 1264-1276 (2007).

Assembly members:
CAC monomer, polymer, 87 residues, 9567.128 Da.

Natural source:   Common Name: HIV   Taxonomy ID: 11676   Superkingdom: Viruses   Kingdom: not available   Genus/species: Lentivirus HIV

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

Entity Sequences (FASTA):
CAC monomer: MSPTSILDIRQGPKEPFRDY VDRFYKTLRAEQASQEVKNA MTETLLVQNANPDCKTILKA LGPAATLEEMMTACQGVGGP GHKARVL

Data sets:
Data typeCount
15N chemical shifts68
1H chemical shifts526

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CAC monomer1

Entities:

Entity 1, CAC monomer 87 residues - 9567.128 Da.

1   METSERPROTHRSERILELEUASPILEARG
2   GLNGLYPROLYSGLUPROPHEARGASPTYR
3   VALASPARGPHETYRLYSTHRLEUARGALA
4   GLUGLNALASERGLNGLUVALLYSASNALA
5   METTHRGLUTHRLEULEUVALGLNASNALA
6   ASNPROASPCYSLYSTHRILELEULYSALA
7   LEUGLYPROALAALATHRLEUGLUGLUMET
8   METTHRALACYSGLNGLYVALGLYGLYPRO
9   GLYHISLYSALAARGVALLEU

Samples:

sample_1: entity, [U-15N], 1 mM; potassium phosphate, none, 100 mM; TSP, none, 0.00001 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D NOESYsample_1isotropicsample_conditions_1
2D TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, P Guntert, C Mumenthaler and K Wuthrich - structure solution

SPARKY v3.0, T Goddard - chemical shift assignment, peak picking

AMBER v8, DA Case, TA Darden, TE Cheatham, III, CL Simmerling, J Wang, RE Duke, - refinement

xwinnmr, Bruker Biospin - collection

NMR spectrometers:

  • Bruker DRX 500 MHz

Related Database Links:

BMRB 16555 17307 17738 19261 19264 19575 25532
PDB
DBJ BAA00992 BAA12988 BAA12996 BAA93773 BAA93774
EMBL CAA06946 CAA11880 CAA11886 CAA77621 CAA82791
GB AAA44201 AAA44306 AAA44652 AAA44987 AAA45003
PIR FOVWLV
PRF 1102247B 1103299C
REF NP_057849 NP_057850 NP_579880
SP P03347 P03348 P03349 P03366 P03367