BMRB Entry 19264

Title:
The structure of the W184AM185A mutant of the HIV-1 capsid protein
Deposition date:
2013-05-24
Original release date:
2013-11-18
Authors:
Deshmukh, Lalit; Schwieters, Charles; Grishaev, Alexander; Clore, G. Marius; Ghirlando, Rodolfo
Citation:

Citation: Deshmukh, Lalit; Schwieters, Charles; Grishaev, Alexander; Ghirlando, Rodolfo; Baber, James; Clore, G. Marius. "Structure and Dynamics of Full-Length HIV-1 Capsid Protein in Solution."  J. Am. Chem. Soc. 135, 16133-16147 (2013).
PubMed: 24066695

Assembly members:

Assembly members:
entity, polymer, 231 residues, 24479.195 Da.

Natural source:

Natural source:   Common Name: Human Immunodeficiency Virus   Taxonomy ID: 11676   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET11a

Data sets:
Data typeCount
13C chemical shifts648
15N chemical shifts206
1H chemical shifts206

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1W184AM185A mutant of the HIV-1 capsid protein1

Entities:

Entity 1, W184AM185A mutant of the HIV-1 capsid protein 231 residues - 24479.195 Da.

1   PROILEVALGLNASNLEUGLNGLYGLNMET
2   VALHISGLNALAILESERPROARGTHRLEU
3   ASNALATRPVALLYSVALVALGLUGLULYS
4   ALAPHESERPROGLUVALILEPROMETPHE
5   SERALALEUSERGLUGLYALATHRPROGLN
6   ASPLEUASNTHRMETLEUASNTHRVALGLY
7   GLYHISGLNALAALAMETGLNMETLEULYS
8   GLUTHRILEASNGLUGLUALAALAGLUTRP
9   ASPARGLEUHISPROVALHISALAGLYPRO
10   ILEALAPROGLYGLNMETARGGLUPROARG
11   GLYSERASPILEALAGLYTHRTHRSERTHR
12   LEUGLNGLUGLNILEGLYTRPMETTHRHIS
13   ASNPROPROILEPROVALGLYGLUILETYR
14   LYSARGTRPILEILELEUGLYLEUASNLYS
15   ILEVALARGMETTYRSERPROTHRSERILE
16   LEUASPILEARGGLNGLYPROLYSGLUPRO
17   PHEARGASPTYRVALASPARGPHETYRLYS
18   THRLEUARGALAGLUGLNALASERGLNGLU
19   VALLYSASNALAALATHRGLUTHRLEULEU
20   VALGLNASNALAASNPROASPCYSLYSTHR
21   ILELEULYSALALEUGLYPROGLYALATHR
22   LEUGLUGLUMETMETTHRALACYSGLNGLY
23   VALGLYGLYPROGLYHISLYSALAARGVAL
24   LEU

Samples:

sample_1: entity, [U-13C; U-15N; U-2H], 0.5 mM; EDTA 1 mM; sodium chloride 50 mM; DTT 1 mM; sodium phosphate 20 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D TROSY-Artsysample_1isotropicsample_conditions_1
2D 1H-15N R1sample_1isotropicsample_conditions_1
2D 1H-15N R1sample_1isotropicsample_conditions_1
2D 1H-15N R1rsample_1isotropicsample_conditions_1
2D 1H-15N R1rsample_1isotropicsample_conditions_1
2D 1H-15N HetNOEsample_1isotropicsample_conditions_1
2D 1H-15N HetNOEsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH v2.32, Schwieters, Kuszewski, Tjandra and Clore - refinement

TOPSPIN v1.3, Bruker Biospin - collection

CCPN-Analysis v2.2.2, (CCPN-Analysis)-Vranken, Boucher, Stevens..Laue. - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 500 MHz

Related Database Links:

BMRB 17738 19261 19575 25532
PDB
DBJ BAA00992 BAA12988 BAA12996 BAA93773 BAA93775
EMBL CAA11884 CAA25902 CAA65355 CAA76038 CAB85858
GB AAA44201 AAA44652 AAA44987 AAA45003 AAA45091
PIR FOVWLV
PRF 1102247B 1103299C
REF NP_057849 NP_057850 NP_579880
SP P03347 P03348 P03349 P03366 P03367
AlphaFold P03347 P03348 P03349 P03366 P03367

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