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 1A43 1AUM 1BAJ 1E6J 1VU4 1VU5 1VU6 1VU7 1VU8 1VU9 1VUA 1VUC 1VUD 1VUE 1VUF 1VUG 1VUH 1VUI 1VUJ 1VUK 1VUL 1VUM 1VUN 1VUO 1VUP 1VUQ 1VUR 1VUS 1VUT 1VUU 1VUV 1VUW 1VUX 1VUY 1VUZ 1VV0 1VV1 1VV2 1VV3 1VV4 1VV5 1VV6 1VV7 1VV8 1VV9 1VVA 1VVB 1VVF 1VVG 1VVH 1VVI 2BUO 2JO0 2JYG 2JYL 2KOD 2L6E 2LF4 2M8L 2M8N 2M8P 2XT1 2XV6 2XXM 3DIK 3GV2 3H47 3H4E 3J34 3J4F 3LRY 3MGE 3NTE 3P05 3P0A 4ARG 4IPY 4QNB 4U0A 4U0B 4U0C 4U0D 4U0E 4U0F 4WYM 4XFX 4XFY 4XFZ
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