BMRB Entry 6823

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR6823

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Title:
Backbone and Sidechain chemical shift assignments of the Human Rhinovirus 3C Protease covalently complexed with a peptidyl inhibitor
Deposition date:
2005-09-12
Original release date:
2006-10-26
Authors:
Bjorndahl, Trent; Andrew, Lena; Wishart, David
Citation:

Citation: Bjorndahl, Trent; Andrew, Lena; Semenchenko, Valentyna; Wishart, David. "NMR Solution Structures of the Apo and Peptide-Inhibited Human Rhinovirus 3C Protease (Serotype 14): Structural and Dynamic Comparison"  Biochemistry 46, 12945-12958 (2007).
PubMed: 17944485

Assembly members:

Assembly members:
HRV14-3C protease with Acetyl-LEALFQ-ethylpropeonate, polymer, 182 residues, 20813.67 Da.
Acetyl-LEALFQ-ethylpropeonate, polymer, 8 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: rhinovirus   Taxonomy ID: 12131   Superkingdom: Viruses   Kingdom: Not applicable   Genus/species: Rhinovirus Human Rhinovirus B

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HRV14-3C protease with Acetyl-LEALFQ-ethylpropeonate: GPNTEFALSLLRKNIMTITT SKGEFTGLGIHDRVCVIPTH AQPGDDVLVNGQKIRVKDKY KLVDPENINLELTVLTLDRN EKFRDIRGFISEDLEGVDAT LVVHSNNFTNTILEVGPVTM AGLINLSSTPTNRMIRYDYA TKTGQCGGVLCATGKIFGIH VGGNGRQGFSAQLKKQYFVE KQ
Acetyl-LEALFQ-ethylpropeonate: XLEALFQX

Data sets:
Data typeCount
13C chemical shifts802
15N chemical shifts184
1H chemical shifts1335

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HRV1
2LEALFQ2

Entities:

Entity 1, HRV 182 residues - 20813.67 Da.

1   GLYPROASNTHRGLUPHEALALEUSERLEU
2   LEUARGLYSASNILEMETTHRILETHRTHR
3   SERLYSGLYGLUPHETHRGLYLEUGLYILE
4   HISASPARGVALCYSVALILEPROTHRHIS
5   ALAGLNPROGLYASPASPVALLEUVALASN
6   GLYGLNLYSILEARGVALLYSASPLYSTYR
7   LYSLEUVALASPPROGLUASNILEASNLEU
8   GLULEUTHRVALLEUTHRLEUASPARGASN
9   GLULYSPHEARGASPILEARGGLYPHEILE
10   SERGLUASPLEUGLUGLYVALASPALATHR
11   LEUVALVALHISSERASNASNPHETHRASN
12   THRILELEUGLUVALGLYPROVALTHRMET
13   ALAGLYLEUILEASNLEUSERSERTHRPRO
14   THRASNARGMETILEARGTYRASPTYRALA
15   THRLYSTHRGLYGLNCYSGLYGLYVALLEU
16   CYSALATHRGLYLYSILEPHEGLYILEHIS
17   VALGLYGLYASNGLYARGGLNGLYPHESER
18   ALAGLNLEULYSLYSGLNTYRPHEVALGLU
19   LYSGLN

Entity 2, LEALFQ 8 residues - Formula weight is not available

1   ACELEUGLUALALEUPHEGLNCA1

Samples:

sample_1: HRV14-3C protease with Acetyl-LEALFQ-ethylpropeonate, [U-90%13C; U-90% 15N], 0.75 mM; HRV14-3C protease with Acetyl-LEALFQ-ethylpropeonate 0.75 mM

conditions_1: ionic strength: 20 mM; pH: 6.5; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1N15N HSQCsample_1not availableconditions_1
1N13C HSQCsample_1not availableconditions_1
HNCAsample_1not availableconditions_1
HNCACBsample_1not availableconditions_1
CBCACONNHsample_1not availableconditions_1
HBHACONNHsample_1not availableconditions_1
CCH-TOCSYsample_1not availableconditions_1
HCCH-TOCSYsample_1not availableconditions_1
HNCOsample_1not availableconditions_1
15N-NOESY-HSQCsample_1not availableconditions_1
13C-NOESY-HSQCsample_1not availableconditions_1
HCCONNHsample_1not availableconditions_1
HNHAsample_1not availableconditions_1
13C15N CHIRPsample_1not availableconditions_1
13C15N Filtered TOCSYsample_1not availableconditions_1
CCONNHsample_1not availableconditions_1

Software:

VNMR v6.1c, Varian - data collection

NMRPipe, NIH - data processing

NMRDraw v5.2.2 - data analysis

NMR spectrometers:

  • Varian Inova 500 MHz

Related Database Links:

PDB
EMBL CAA25565
GB AAA45756 AAA45757 AAA45758
REF NP_041009 NP_740524
SP P03303
AlphaFold P03303

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