BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16341

Title: The inactive form of the retroviral protease of the murine intracisternal particle, inMIA-14 PR   PubMed: 19856131

Deposition date: 2009-06-09 Original release date: 2009-11-16

Authors: Motackova, Veronika; Kubickova, Monika; Kozisek, Milan; Grantz-Saskova, Klara; Svec, Martin; Zidek, Lukas; Sklenar, Vladimir

Citation: Motakova, Veronika; Kubikova, Monika; Kozisek, Milan; Sakova, Klara; Svec, Martin; Zidek, Luka; Sklena, Vladimir. "Backbone (1)H, (13)C, and (15)N NMR assignment for the inactive form of the retroviral protease of the murine intracisternal A-type particle, inMIA-14 PR."  Biomol NMR Assign 3, 261-264 (2009).

Assembly members:
inMIA14-PR, polymer, 156 residues, Formula weight is not available

Natural source:   Common Name: Murine endogenous retrovirus   Taxonomy ID: 35275   Superkingdom: Viruses   Kingdom: not available   Genus/species: Betaretrovirus Murine endogenous retrovirus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22

Entity Sequences (FASTA):
inMIA14-PR: LVVSLNDRPKLRLKINGKEF EGILDTGADKSIISTHWWPK AWPTTESSHSLQGLGYQSCP TISSVALTWESSEGQQGKFI PYVLPLPVNLWGRDIMQHLG LILSNENAPSGGYSTKAKNI MAKMGYKEGKGLGHQEQGRI EPISPNGNQDRQGLGF

Data sets:
Data typeCount
13C chemical shifts416
15N chemical shifts135
1H chemical shifts135

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1inMIA14-PR1

Entities:

Entity 1, inMIA14-PR 156 residues - Formula weight is not available

1   LEUVALVALSERLEUASNASPARGPROLYS
2   LEUARGLEULYSILEASNGLYLYSGLUPHE
3   GLUGLYILELEUASPTHRGLYALAASPLYS
4   SERILEILESERTHRHISTRPTRPPROLYS
5   ALATRPPROTHRTHRGLUSERSERHISSER
6   LEUGLNGLYLEUGLYTYRGLNSERCYSPRO
7   THRILESERSERVALALALEUTHRTRPGLU
8   SERSERGLUGLYGLNGLNGLYLYSPHEILE
9   PROTYRVALLEUPROLEUPROVALASNLEU
10   TRPGLYARGASPILEMETGLNHISLEUGLY
11   LEUILELEUSERASNGLUASNALAPROSER
12   GLYGLYTYRSERTHRLYSALALYSASNILE
13   METALALYSMETGLYTYRLYSGLUGLYLYS
14   GLYLEUGLYHISGLNGLUGLNGLYARGILE
15   GLUPROILESERPROASNGLYASNGLNASP
16   ARGGLNGLYLEUGLYPHE

Samples:

sample_1: inMIA14-PR, [U-100% 13C; U-100% 15N; U-75% 2H], 0.3 mM; sodium chloride 50 mM; sodium azide 50 uM; phosphate buffer 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 7.4; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1

Software:

NMRPipe v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

DBJ BAC79171
EMBL CRH48730 CRH55731 CRH56783 CRH57961
GB AAC12789 AAC52922
REF WP_057247684 WP_057256782
SP P11365

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts