BMRB Entry 19072

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19072

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignment for inactive HIV-1 protease Bmut5
Deposition date:
2013-03-04
Original release date:
2013-03-13
Authors:
Huang, Xi; Fanucci, Gail
Citation:

Citation: Huang, Xi; de Vera, Ian Mitchelle S; Veloro, Angelo; Rocca, James; Simmerling, Carlos; Dunn, Ben; Fanucci, Gail. "Backbone H, C, and N chemical shift assignment for HIV-1 protease subtypes and multi-drug resistant variant MDR 769."  Biomol. NMR Assignments 7, 199-202 (2013).
PubMed: 22752791

Assembly members:

Assembly members:
HIV-1_PR_Homodimer_Bmut5, polymer, 99 residues, 21115.04 Da.

Natural source:

Natural source:   Common Name: HIV-1   Taxonomy ID: 11676   Superkingdom: Viruses   Kingdom: not available   Genus/species: Lentivirus HIV-1

Experimental source:

Experimental source:   Production method: chemical synthesis   Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HIV-1_PR_Homodimer_Bmut5: PQITLWKRPLVTIKVGGQLK EALLNTGADDTVIEDMNLPG KWKPKMIGGIGGFIKVKQYD QIIIEIAGHKAIGTVLVGPT PVNIIGRNLLTQIGATLNF

Data sets:
Data typeCount
heteronuclear NOE values89
T1 relaxation values89
T2 relaxation values89

Additional metadata:

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  • Samples and Experiments
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Assembly:

Entity Assembly IDEntity NameEntity ID
1HIV-1 Protease Bmut5, 11
2HIV-1 Protease Bmut5, 21

Entities:

Entity 1, HIV-1 Protease Bmut5, 1 99 residues - 21115.04 Da.

1   PROGLNILETHRLEUTRPLYSARGPROLEU
2   VALTHRILELYSVALGLYGLYGLNLEULYS
3   GLUALALEULEUASNTHRGLYALAASPASP
4   THRVALILEGLUASPMETASNLEUPROGLY
5   LYSTRPLYSPROLYSMETILEGLYGLYILE
6   GLYGLYPHEILELYSVALLYSGLNTYRASP
7   GLNILEILEILEGLUILEALAGLYHISLYS
8   ALAILEGLYTHRVALLEUVALGLYPROTHR
9   PROVALASNILEILEGLYARGASNLEULEU
10   THRGLNILEGLYALATHRLEUASNPHE

Related Database Links:

BMRB 17994