BMRB Entry 16555

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16555

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
1H, 15N and 13C assignments of the dimeric C-terminal domain of HIV-1 capsid protein
Deposition date:
2009-10-15
Original release date:
2009-11-30
Authors:
Jung, Jinwon; Byeon, In-Ja; Ahn, Jinwoo; Concel, Jason; Gronenborn, Angela
Citation:

Citation: Jung, Jinwon; Byeon, In-Ja; Ahn, Jinwoo; Concel, Jason; Gronenborn, Angela. "1H, 15N and 13C assignments of the dimeric C-terminal domain of HIV-1 capsid protein."  Biomol. NMR Assignments 4, 21-23 (2010).
PubMed: 19921549

Assembly members:

Assembly members:
HIV-1_Capsid_Protein, polymer, 88 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Lentivirus human immunodeficiency virus   Taxonomy ID: 11646   Superkingdom: Viruses   Kingdom: not available   Genus/species: Lentivirus HIV-1

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HIV-1_Capsid_Protein: MYSPTSILDIRQGPKEPFRD YVDRFYKTLRAEQASQEVKN WMTETLLVQNANPDCKTILK ALGPAATLEEMMTACQGVGG PGHKARVL

Data sets:
Data typeCount
13C chemical shifts272
15N chemical shifts91
1H chemical shifts568

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit 11
2subunit 21

Entities:

Entity 1, subunit 1 88 residues - Formula weight is not available

1   METTYRSERPROTHRSERILELEUASPILE
2   ARGGLNGLYPROLYSGLUPROPHEARGASP
3   TYRVALASPARGPHETYRLYSTHRLEUARG
4   ALAGLUGLNALASERGLNGLUVALLYSASN
5   TRPMETTHRGLUTHRLEULEUVALGLNASN
6   ALAASNPROASPCYSLYSTHRILELEULYS
7   ALALEUGLYPROALAALATHRLEUGLUGLU
8   METMETTHRALACYSGLNGLYVALGLYGLY
9   PROGLYHISLYSALAARGVALLEU

Samples:

sample_1: HIV-1 CA-CTD, [U-100% 13C; U-100% 15N], 2 mM; H2O 93%; D2O 7%; sodium phosphate 25 mM; sodium azide 0.02%; DTT 2 mM

sample_conditions_1: ionic strength: 25 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D simultaneous 13C,15N-edited NOESYsample_1isotropicsample_conditions_1
3D 13C-edited NOESYsample_1isotropicsample_conditions_1
2D NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz

Related Database Links:

BMRB 15137 17307 19261 19575 25532
PDB
DBJ BAA00992 BAA12988 BAA12996 BAA93773 BAA93774
EMBL CAA06946 CAA11880 CAA11884 CAA11886 CAA12915
GB AAA44201 AAA44224 AAA44225 AAA44306 AAA44652
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