BMRB Entry 25292

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25292

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Title:
HIV-1 reverse transcriptase N terminal 216 residues (Fingers and Palm subdomain)
Deposition date:
2014-10-21
Original release date:
2014-11-21
Authors:
Zheng, Xunhai; Mueller, Geoffry; London, Robert
Citation:

Citation: Zheng, Xunhai; Pedersen, Lars; Gabel, Scott; Mueller, Geoffrey; Cuneo, Matthew; DeRose, Eugene; Krahn, Juno; London, Robert. "Selective unfolding of one Ribonuclease H domain of HIV reverse transcriptase is linked to homodimer formation"  Nucleic Acids Res. 42, 5361-5377 (2014).
PubMed: 24574528

Assembly members:

Assembly members:
RT216, polymer, 217 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PET30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RT216: MPISPIETVPVKLKPGMDGP KVKQWPLTEEKIKALVEICT EMEKEGKISKIGPENPYNTP VFAIKKKDSTKWRKLVDFRE LNKRTQDFWEVQLGIPHPAG LKKKKSVTVLDVGDAYFSVP LDEDFRKYTAFTIPSINNET PGIRYQYNVLPQGWKGSPAI FQSSMTKILEPFRKQNPDIV IYQYMDDLYVGSDLEIGQHR TKIEELRQHLLRWGLTT

Data sets:
Data typeCount
13C chemical shifts284
15N chemical shifts131
1H chemical shifts131

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RT2161

Entities:

Entity 1, RT216 217 residues - Formula weight is not available

1   METPROILESERPROILEGLUTHRVALPRO
2   VALLYSLEULYSPROGLYMETASPGLYPRO
3   LYSVALLYSGLNTRPPROLEUTHRGLUGLU
4   LYSILELYSALALEUVALGLUILECYSTHR
5   GLUMETGLULYSGLUGLYLYSILESERLYS
6   ILEGLYPROGLUASNPROTYRASNTHRPRO
7   VALPHEALAILELYSLYSLYSASPSERTHR
8   LYSTRPARGLYSLEUVALASPPHEARGGLU
9   LEUASNLYSARGTHRGLNASPPHETRPGLU
10   VALGLNLEUGLYILEPROHISPROALAGLY
11   LEULYSLYSLYSLYSSERVALTHRVALLEU
12   ASPVALGLYASPALATYRPHESERVALPRO
13   LEUASPGLUASPPHEARGLYSTYRTHRALA
14   PHETHRILEPROSERILEASNASNGLUTHR
15   PROGLYILEARGTYRGLNTYRASNVALLEU
16   PROGLNGLYTRPLYSGLYSERPROALAILE
17   PHEGLNSERSERMETTHRLYSILELEUGLU
18   PROPHEARGLYSGLNASNPROASPILEVAL
19   ILETYRGLNTYRMETASPASPLEUTYRVAL
20   GLYSERASPLEUGLUILEGLYGLNHISARG
21   THRLYSILEGLUGLULEUARGGLNHISLEU
22   LEUARGTRPGLYLEUTHRTHR

Samples:

sample_1: RT216, [U-13C; U-15N; U-2H] ILE methyl protonated, .6 mM; TRIS, d-11, 50 mM; EDTA, d-16, 1 mM; DSS 0.2 mM; sodium azide 2%; H2O 90%; D2O 8%

sample_conditions_1: ionic strength: 1 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CA)CBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CCCCOSY_CA_NNHsample_1isotropicsample_conditions_1
3D HCCCCOSY_CA_NNHsample_1isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - data analysis

VNMRJ, Varian - collection

NMR spectrometers:

  • Varian INOVA 600 MHz

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