BMRB Entry 50541

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR50541

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Title:
13C and 15N Chemical Shift Assignments for the Tubular Assembly of the Rous Sarcoma Virus Capsid Protein
Deposition date:
2020-10-29
Original release date:
2020-11-05
Authors:
Jeon, Jaekyun; Qiao, Xin; Hung, Ivan; Mitra, Alok; Desfosses, Ambroise; Huang, Daniel; Gor'kov, Peter; Craven, Rebecca; Kingston, Richard; Gan, Zhehong; Zhu, Fangqiang; Chen, Bo
Citation:

Citation: Jeon, Jaekyun; Qiao, Xin; Hung, Ivan; Mitra, Alok; Desfosses, Ambroise; Huang, Daniel; Gor'kov, Peter; Craven, Rebecca; Kingston, Richard; Gan, Zhehong; Zhu, Fangqiang; Chen, Bo. "Structural Model of the Tubular Assembly of the Rous Sarcoma Virus Capsid Protein."  J. Am. Chem. Soc. 139, 2006-2013 (2017).
PubMed: 28094514

Assembly members:

Assembly members:
entity_1, polymer, 237 residues, 25550 Da.

Natural source:

Natural source:   Common Name: Rous sarcoma virus   Taxonomy ID: 11886   Superkingdom: Viruses   Kingdom: not available   Genus/species: Alpharetrovirus Rous sarcoma virus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-24(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: PVVIKTEGPAWTPLEPKLIT RLADTVRTKGLRSPITMAEV EALMSSPLLPHDVTNLMRVI LGPAPYALWMDAWGVQLQTV IAAATRDPRHPANGQGRGER TNLNRLKGLADGMVGNPQGQ AALLRPGELVAITASALQAF REVARLAEPAGPWADIMQGP SESFVDFANRLIKAVEGSDL PPSARAPVIIDCFRQKSQPD IQQLIRTAPSTLTTPGEIIK YVLDRQKTAPLTDQGIA

Data sets:
Data typeCount
13C chemical shifts1042
15N chemical shifts226

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rous Sarcoma Virus Capsid Protein, Monomer 11
2Rous Sarcoma Virus Capsid Protein, Monomer 21
3Rous Sarcoma Virus Capsid Protein, Monomer 31
4Rous Sarcoma Virus Capsid Protein, Monomer 41
5Rous Sarcoma Virus Capsid Protein, Monomer 51
6Rous Sarcoma Virus Capsid Protein, Monomer 61

Entities:

Entity 1, Rous Sarcoma Virus Capsid Protein, Monomer 1 237 residues - 25550 Da.

1   PROVALVALILELYSTHRGLUGLYPROALA
2   TRPTHRPROLEUGLUPROLYSLEUILETHR
3   ARGLEUALAASPTHRVALARGTHRLYSGLY
4   LEUARGSERPROILETHRMETALAGLUVAL
5   GLUALALEUMETSERSERPROLEULEUPRO
6   HISASPVALTHRASNLEUMETARGVALILE
7   LEUGLYPROALAPROTYRALALEUTRPMET
8   ASPALATRPGLYVALGLNLEUGLNTHRVAL
9   ILEALAALAALATHRARGASPPROARGHIS
10   PROALAASNGLYGLNGLYARGGLYGLUARG
11   THRASNLEUASNARGLEULYSGLYLEUALA
12   ASPGLYMETVALGLYASNPROGLNGLYGLN
13   ALAALALEULEUARGPROGLYGLULEUVAL
14   ALAILETHRALASERALALEUGLNALAPHE
15   ARGGLUVALALAARGLEUALAGLUPROALA
16   GLYPROTRPALAASPILEMETGLNGLYPRO
17   SERGLUSERPHEVALASPPHEALAASNARG
18   LEUILELYSALAVALGLUGLYSERASPLEU
19   PROPROSERALAARGALAPROVALILEILE
20   ASPCYSPHEARGGLNLYSSERGLNPROASP
21   ILEGLNGLNLEUILEARGTHRALAPROSER
22   THRLEUTHRTHRPROGLYGLUILEILELYS
23   TYRVALLEUASPARGGLNLYSTHRALAPRO
24   LEUTHRASPGLNGLYILEALA

Samples:

sample_1: Capsid Protein, [U-100% 13C; U-100% 15N], 20 mg/mL; sodium phosphate 50 mM; polyethylene glycol 8000 20 w/v

sample_2: Capsid Protein, 1,3 13C Glycerol, 20 mg/mL; sodium phosphate 50 mM; polyethylene glycol 8000 20 w/v

sample_3: Capsid Protein, 2 13C Glycerol, 20 mg/mL; sodium phosphate 50 mM; polyethylene glycol 8000 20 w/v

sample_4: Capsid Protein, [U-13C; U-15N]-Leu, 20 mg/mL; sodium phosphate 50 mM; polyethylene glycol 8000 20 w/v

sample_5: Capsid Protein, [U-15N]-Leu, 20 mg/mL; sodium phosphate 50 mM; polyethylene glycol 8000 20 w/v

sample_conditions_1: pH: 8.0; temperature: 277 K

Experiments:

NameSampleSample stateSample conditions
2D 13C-13C DARRsample_1isotropicsample_conditions_1
2D 13C/13C TOBSYsample_1isotropicsample_conditions_1
2D NCACXsample_1isotropicsample_conditions_1
2D NCOCXsample_1isotropicsample_conditions_1
3D NCACXsample_1isotropicsample_conditions_1
3D NCOCXsample_1isotropicsample_conditions_1
3D CaNCOCxsample_1isotropicsample_conditions_1
2D 13C-13C DARRsample_2isotropicsample_conditions_1
2D NCaCxsample_2isotropicsample_conditions_1
2D NCOCxsample_2isotropicsample_conditions_1
3D NCACXsample_2isotropicsample_conditions_1
3D NCOCXsample_2isotropicsample_conditions_1
2D 13C-13C DARRsample_3isotropicsample_conditions_1
2D NCaCxsample_3isotropicsample_conditions_1
2D NCOCxsample_3isotropicsample_conditions_1
3D NCACXsample_3isotropicsample_conditions_1
3D NCOCXsample_3isotropicsample_conditions_1
2D NCACXsample_5isotropicsample_conditions_1
2D NCOCXsample_5isotropicsample_conditions_1
2D NCACXsample_4isotropicsample_conditions_1
2D NCOCXsample_4isotropicsample_conditions_1

Software:

VNMRj v4.0 - collection

NMRPipe - processing

NMRFAM-SPARKY v1.470 - peak picking

mcassign2 - chemical shift assignment

NMR spectrometers:

  • Agilent DDR2 600 MHz
  • Brucker Avance 600 MHz
  • Brucker Avance 900 MHz