BMRB Entry 15277

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15277
MolProbity Validation Chart

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Title:
Full Length Leader Protease of Foot and Mouth Disease Virus C51A Mutant
Deposition date:
2007-06-01
Original release date:
2007-07-05
Authors:
Cencic, Regina; Mayer, Christina; Juliano, Maria; Juliano, Luiz; Konrat, Robert; Kontaxis, Georg; Skern, Tim
Citation:

Citation: Cencic, Regina; Mayer, Christina; Juliano, Maria; Juliano, Luiz; Konrat, Robert; Kontaxis, Georg; Skern, Tim. "Investigating the substrate specificity and oligomerisation of the leader protease of foot and mouth disease virus using NMR"  J. Mol. Biol. 373, 1071-1087 (2007).
PubMed: 17897674

Assembly members:

Assembly members:
Lbpro, polymer, 173 residues, 38529.820 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 12110   Superkingdom: Viruses   Kingdom: not available   Genus/species: Aphthovirus Foot-and-mouth disease virus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET8c

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Lbpro: MELTLYNGEKKTFYSRPNNH DNAWLNAILQLFRYVEEPFF DWVYSSPENLTLEAIKQLED LTGLELHEGGPPALVIWNIK HLLHTGIGTASRPSEVCVVD GTDMCLADFHAGIFLKGQEH AVFACVTSNGWYAIDDEDFY PWTPDPSDVLVFVPYDQEPL NGEWKAKVQRKLK

Data sets:
Data typeCount
13C chemical shifts286
15N chemical shifts131
1H chemical shifts131

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Leader Protease1

Entities:

Entity 1, Leader Protease 173 residues - 38529.820 Da.

1   METGLULEUTHRLEUTYRASNGLYGLULYS
2   LYSTHRPHETYRSERARGPROASNASNHIS
3   ASPASNALATRPLEUASNALAILELEUGLN
4   LEUPHEARGTYRVALGLUGLUPROPHEPHE
5   ASPTRPVALTYRSERSERPROGLUASNLEU
6   THRLEUGLUALAILELYSGLNLEUGLUASP
7   LEUTHRGLYLEUGLULEUHISGLUGLYGLY
8   PROPROALALEUVALILETRPASNILELYS
9   HISLEULEUHISTHRGLYILEGLYTHRALA
10   SERARGPROSERGLUVALCYSVALVALASP
11   GLYTHRASPMETCYSLEUALAASPPHEHIS
12   ALAGLYILEPHELEULYSGLYGLNGLUHIS
13   ALAVALPHEALACYSVALTHRSERASNGLY
14   TRPTYRALAILEASPASPGLUASPPHETYR
15   PROTRPTHRPROASPPROSERASPVALLEU
16   VALPHEVALPROTYRASPGLNGLUPROLEU
17   ASNGLYGLUTRPLYSALALYSVALGLNARG
18   LYSLEULYS

Samples:

sample_1: Leader Protease, [U-100% 13C; U-100% 15N], 1 mM; DTT 5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 10 mM; H2O 90%; D2O 10%

sample_2: Leader Protease, [U-100% 15N], 1 mM; DTT 5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 10 mM; H2O 90%; D2O 10%

sample_3: Leader Protease, [U-100% 15N], 1 mM; DTT 5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 10 mM; Pf1 phage 17 mg/ml; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-15N IPAP HSQCsample_2isotropicsample_conditions_1
2D 1H-15N IPAP HSQCsample_3anisotropicsample_conditions_1

Software:

VNMR v6.1C, Varian - collection

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

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - peak picking

SPARKY, Goddard - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 800 MHz
  • Varian Direct Drive 600 MHz

Related Database Links:

BMRB 15278
PDB
EMBL CAA25416 CAC86575
GB AAT01757 AAT01758 AAT01759 AAT01760 AAT01761
PIR GNNYF
SP P03305
AlphaFold P03305

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